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Reviewed, UniProtKB/Swiss-Prot Q91WQ3 (SYYC_MOUSE)

Last modified October 13, 2009. Version 67. 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

Names and origin

Protein namesRecommended name:
    Tyrosyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.1
Alternative name(s):
    Tyrosyl--tRNA ligase
      Short name=TyrRS
Gene names
Name: Yars
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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

Cytoplasm By similarity.

Sequence similarities

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

Contains 1 tRNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Gene Ontology (GO)
   Biological processtyrosyl-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

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine-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 – 528527Tyrosyl-tRNA synthetase, cytoplasmic
PRO_0000055674

Regions

Domain364 – 468105tRNA-binding
Motif44 – 529"HIGH" region
Motif222 – 2265"KMSKS" region

Sites

Binding site391Tyrosine By similarity
Binding site1661Tyrosine By similarity
Binding site1701Tyrosine By similarity
Binding site1731Tyrosine By similarity
Binding site1881Tyrosine By similarity

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue1971N6-acetyllysine By similarity
Modified residue2061N6-acetyllysine By similarity
Modified residue2721N6-acetyllysine By similarity
Modified residue4741N6-acetyllysine By similarity
Modified residue4821N6-acetyllysine By similarity
Modified residue4901N6-acetyllysine By similarity

Experimental info

Sequence conflict111L → M in BAC26120. Ref.1
Sequence conflict291E → K in BAE24073. Ref.1
Sequence conflict1951A → S in BAC36424. Ref.1
Sequence conflict2941E → Q in BAC36424. Ref.1
Sequence conflict3201L → W in BAC36424. Ref.1
Sequence conflict3771S → R in BAC36424. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91WQ3-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 39D852D4C5701D0B

FASTA52859,105
        10         20         30         40         50         60 
MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKVYW GTATTGKPHV AYFVPMSKIA 

        70         80         90        100        110        120 
DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRTSYYENV IKAMLESIGV PLEKLKFIKG 

       130        140        150        160        170        180 
TDYQLSKEYT LDVYRLSSVV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD 

       190        200        210        220        230        240 
AQFGGVDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED 

       250        260        270        280        290        300 
VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT VYLELEKDFA 

       310        320        330        340        350        360 
AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPP AKGPAKNSEP 

       370        380        390        400        410        420 
EEVIPSRLDI RVGKILSVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV 

       430        440        450        460        470        480 
VVLCNLKPQK MRGVDSQGML LCASVEGVSR QVEPLDPPAG SAPGERVFVQ GYEKGQPDEE 

       490        500        510        520 
LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGFVSCK SLKGGNIS 

« 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 and NOD.
Tissue: Bone marrow, Brain cortex, Egg, Embryo, Skin, Testis and Thymus.
[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: Kidney and Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK028785 mRNA. Translation: BAC26120.1.
AK043837 mRNA. Translation: BAC31674.1.
AK076634 mRNA. Translation: BAC36424.1.
AK139579 mRNA. Translation: BAE24073.1.
AK145356 mRNA. Translation: BAE26384.1.
AK151880 mRNA. Translation: BAE30766.1.
AK169708 mRNA. Translation: BAE41320.1.
BC013552 mRNA. Translation: AAH13552.1.
BC022143 mRNA. Translation: AAH22143.1.
BC026615 mRNA. Translation: AAH26615.1.
IPIIPI00314153.
RefSeqNP_598912.3.
UniGeneMm.145488
Mm.410673

3D structure databases

HSSPHSSP built from PDB template 1N3L based on UniProtKB P54577.
SMRQ91WQ3. Positions 3-341, 4-342, 359-527, 360-528.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ91WQ3.

PTM databases

PhosphoSiteQ91WQ3.

Proteomic databases

PRIDEQ91WQ3.

Genome annotation databases

EnsemblENSMUST00000001365; ENSMUSP00000001365; ENSMUSG00000028811; Mus musculus. [Genome view]
ENSMUST00000106054; ENSMUSP00000101669; ENSMUSG00000028811; Mus musculus. [Genome view]
GeneID107271.
KEGGmmu:107271.
NMPDRfig|10090.3.peg.10424.
UCSCuc008uwk.1. mouse.

Organism-specific databases

CTD107271.
MGIMGI:2147627. Yars.

Phylogenomic databases

HOGENOMQ91WQ3.
HOVERGENQ91WQ3.

Enzyme and pathway databases

BRENDA6.1.1.1. 244.

Gene expression databases

ArrayExpressQ91WQ3.
BgeeQ91WQ3.
CleanExMM_YARS.
GenevestigatorQ91WQ3.
GermOnlineENSMUSG00000028811. Mus musculus.

Family and domain databases

InterProIPR002305. aa-tRNA-synth_Ib.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA_bd.
IPR015624. Tyr-tRNA-synth_Ib_arc/euk.
IPR002307. Tyr-tRNA-synth_Ib_bac/mito.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF8. Tyr-tRNA_synth. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio358652.
SOURCESearch...

Entry information

Entry nameSYYC_MOUSE
AccessionPrimary (citable) accession number: Q91WQ3
Secondary accession number(s): Q3TEC8 expand/collapse secondary AC list , Q3U9A1, Q3UTA7, Q8BVT2, Q8C183
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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