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Q91WQ3 (SYYC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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

Names and origin

Protein namesRecommended name:
Tyrosine--tRNA ligase, cytoplasmic

EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS
Gene names
Name:Yars
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtyrosyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Tyrosine--tRNA ligase, cytoplasmic
PRO_0000055674
Initiator methionine11Removed; alternate By similarity
Chain2 – 528527Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed
PRO_0000423286

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 residue11N-acetylmethionine By similarity
Modified residue21N-acetylglycine; in Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed By similarity
Modified residue1971N6-acetyllysine By similarity
Modified residue2061N6-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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney and Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_598912.4. NM_134151.4.
UniGeneMm.145488.

3D structure databases

ProteinModelPortalQ91WQ3.
SMRQ91WQ3. Positions 4-342, 360-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223230. 1 interaction.
IntActQ91WQ3. 2 interactions.
MINTMINT-1855454.

PTM databases

PhosphoSiteQ91WQ3.

Proteomic databases

PaxDbQ91WQ3.
PRIDEQ91WQ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001365; ENSMUSP00000001365; ENSMUSG00000028811.
GeneID107271.
KEGGmmu:107271.
UCSCuc008uwk.2. mouse.

Organism-specific databases

CTD8565.
MGIMGI:2147627. Yars.

Phylogenomic databases

eggNOGCOG0162.
GeneTreeENSGT00750000117748.
HOGENOMHOG000228237.
HOVERGENHBG080113.
InParanoidQ91WQ3.
KOK01866.

Gene expression databases

ArrayExpressQ91WQ3.
BgeeQ91WQ3.
CleanExMM_YARS.
GenevestigatorQ91WQ3.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.50.620. 1 hit.
InterProIPR002305. aa-tRNA-synth_Ic.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR002307. Tyr-tRNA-ligase.
IPR023617. Tyr-tRNA-ligase_arc/euk-type.
[Graphical view]
PANTHERPTHR11946:SF8. PTHR11946:SF8. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01040. TRNASYNTHTYR.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00234. tyrS. 1 hit.
PROSITEPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio358652.
PROQ91WQ3.
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: April 16, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries