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Reviewed, UniProtKB/Swiss-Prot Q8BYL4 (SYYM_MOUSE)

Last modified November 3, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Tyrosyl-tRNA synthetase, mitochondrial
    EC=6.1.1.1
Alternative name(s):
    Tyrosine--tRNA ligase
      Short name=TyrRS
Gene names
Name: Yars2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity.

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processtyrosyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 472Tyrosyl-tRNA synthetase, mitochondrialPRO_0000035831

Regions

Motif77 – 8610"HIGH" region
Motif276 – 2805"KMSKS" region

Sites

Binding site2791ATP By similarity

Amino acid modifications

Modified residue3501N6-acetyllysine By similarity
Modified residue4211Phosphotyrosine By similarity
Modified residue4301Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8BYL4-1 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 7775B040E3E8A2F1

FASTA47252,597
        10         20         30         40         50         60 
MAAPMLRRLC RVPQSLVWLR GSRAVRPGAR GMLVAPRARG LFKEFFPESG TKTELPELFD 

        70         80         90        100        110        120 
RRRAGSSPQT VYCGFDPTGD SLHVGHLLTL LGLFHFQRAG HNVIALVGGS TALLGDPSGR 

       130        140        150        160        170        180 
TKGREALSAE CVRANAHALR RGLEALAANH ARLFADGRPW GSFTVLDNAA WFQEQHLVDF 

       190        200        210        220        230        240 
LATVGGHFRM GTLLSRLSVQ SRLKSPEGMS LAEFFYQVLQ AYDFYYLFQH YGCRVQLGGS 

       250        260        270        280        290        300 
DQLGNIMSGY EFIHKLTGED VFGITVPLIT STTGAKLGKS AGNAVWLNRE KTSPFELYQF 

       310        320        330        340        350        360 
FVRQQDDSVE RYLKLFTFLP LPEIDHIMQL HVKEPEKRVA QKRLAAEVTK LVHGQEGLDS 

       370        380        390        400        410        420 
AKRCTQALYH SSIEALEVMS DQELKELFKE ASFSELVLDP GTSVIDTCRK ANAIPDGPRG 

       430        440        450        460        470 
YRMITEGGVS INHRQVTNPE SVLVIGQHIL KNGLSLLKIG KRNFYIIKWL QL

« Hide

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References

[1]"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: Jaw and Limb.
[2]"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] OF 70-472.
Strain: C57BL/6J.
Tissue: Hypothalamus.
+Additional computationally mapped references.

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Cross-references

Sequence databases

BC060295 mRNA. Translation: AAH60295.1.
AK039123 mRNA. Translation: BAC30245.1.
IPIIPI00396833.
RefSeqNP_937889.1.
UniGeneMm.37486

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BYL4.

PTM databases

PhosphoSiteQ8BYL4.

Proteomic databases

PRIDEQ8BYL4.

Genome annotation databases

EnsemblENSMUST00000059955; ENSMUSP00000055277; ENSMUSG00000022792; Mus musculus. [Genome view]
GeneID70120.
KEGGmmu:70120.
NMPDRfig|10090.3.peg.30910.
UCSCuc007yie.1. mouse.

Organism-specific databases

CTD70120.
MGIMGI:1917370. Yars2.

Phylogenomic databases

HOGENOMQ8BYL4.
HOVERGENQ8BYL4.
OMATFYIGFD.

Enzyme and pathway databases

BRENDA6.1.1.1. 244.

Gene expression databases

ArrayExpressQ8BYL4.
BgeeQ8BYL4.
CleanExMM_YARS2.
GenevestigatorQ8BYL4.
GermOnlineENSMUSG00000022792. Mus musculus.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11766. Tyr_tRNA-synt_1b. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio331028.
SOURCESearch...

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Entry information

Entry nameSYYM_MOUSE
AccessionPrimary (citable) accession number: Q8BYL4
Secondary accession number(s): Q6PAH7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: November 3, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

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