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Protein

Tyrosine--tRNA ligase, cytoplasmic

Gene

Yars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391TyrosineBy similarity
Binding sitei166 – 1661TyrosineBy similarity
Binding sitei170 – 1701TyrosineBy similarity
Binding sitei173 – 1731TyrosineBy similarity
Binding sitei188 – 1881TyrosineBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: MGI
  3. tRNA binding Source: UniProtKB-KW
  4. tyrosine-tRNA ligase activity Source: GO_Central

GO - Biological processi

  1. tyrosyl-tRNA aminoacylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligase, cytoplasmic (EC:6.1.1.1)
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name:
TyrRS
Cleaved into the following chain:
Gene namesi
Name:Yars
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2147627. Yars.

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: GO_Central
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528Tyrosine--tRNA ligase, cytoplasmicPRO_0000055674Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 528527Tyrosine--tRNA ligase, cytoplasmic, N-terminally processedPRO_0000423286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylglycine; in Tyrosine--tRNA ligase, cytoplasmic, N-terminally processedBy similarity
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei206 – 2061N6-acetyllysineBy similarity
Modified residuei474 – 4741N6-acetyllysineBy similarity
Modified residuei482 – 4821N6-acetyllysineBy similarity
Modified residuei490 – 4901N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ91WQ3.
PaxDbiQ91WQ3.
PRIDEiQ91WQ3.

PTM databases

PhosphoSiteiQ91WQ3.

Expressioni

Gene expression databases

BgeeiQ91WQ3.
CleanExiMM_YARS.
ExpressionAtlasiQ91WQ3. baseline and differential.
GenevestigatoriQ91WQ3.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi223230. 1 interaction.
IntActiQ91WQ3. 2 interactions.
MINTiMINT-1855454.

Structurei

3D structure databases

ProteinModelPortaliQ91WQ3.
SMRiQ91WQ3. Positions 4-342, 360-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini364 – 468105tRNA-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi44 – 529"HIGH" region
Motifi222 – 2265"KMSKS" region

Sequence similaritiesi

Contains 1 tRNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0162.
HOGENOMiHOG000228237.
HOVERGENiHBG080113.
InParanoidiQ91WQ3.
KOiK01866.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR002307. Tyr-tRNA-ligase.
[Graphical view]
PfamiPF00579. tRNA-synt_1b. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS50886. TRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91WQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKVYW GTATTGKPHV
60 70 80 90 100
AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRTSYYENV
110 120 130 140 150
IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDAKKAGA
160 170 180 190 200
EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGVDQRK IFTFAEKYLP
210 220 230 240 250
ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC
260 270 280 290 300
EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT VYLELEKDFA
310 320 330 340 350
AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPP
360 370 380 390 400
AKGPAKNSEP EEVIPSRLDI RVGKILSVEK HPDADSLYVE KIDVGEAEPR
410 420 430 440 450
TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVDSQGML LCASVEGVSR
460 470 480 490 500
QVEPLDPPAG SAPGERVFVQ GYEKGQPDEE LKPKKKVFEK LQADFKISEE
510 520
CIAQWKQTNF MTKLGFVSCK SLKGGNIS
Length:528
Mass (Da):59,105
Last modified:January 23, 2007 - v3
Checksum:i39D852D4C5701D0B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → M in BAC26120 (PubMed:16141072).Curated
Sequence conflicti29 – 291E → K in BAE24073 (PubMed:16141072).Curated
Sequence conflicti195 – 1951A → S in BAC36424 (PubMed:16141072).Curated
Sequence conflicti294 – 2941E → Q in BAC36424 (PubMed:16141072).Curated
Sequence conflicti320 – 3201L → W in BAC36424 (PubMed:16141072).Curated
Sequence conflicti377 – 3771S → R in BAC36424 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_598912.4. NM_134151.4.
UniGeneiMm.145488.

Genome annotation databases

GeneIDi107271.
KEGGimmu:107271.
UCSCiuc008uwk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_598912.4. NM_134151.4.
UniGeneiMm.145488.

3D structure databases

ProteinModelPortaliQ91WQ3.
SMRiQ91WQ3. Positions 4-342, 360-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223230. 1 interaction.
IntActiQ91WQ3. 2 interactions.
MINTiMINT-1855454.

PTM databases

PhosphoSiteiQ91WQ3.

Proteomic databases

MaxQBiQ91WQ3.
PaxDbiQ91WQ3.
PRIDEiQ91WQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi107271.
KEGGimmu:107271.
UCSCiuc008uwk.2. mouse.

Organism-specific databases

CTDi8565.
MGIiMGI:2147627. Yars.

Phylogenomic databases

eggNOGiCOG0162.
HOGENOMiHOG000228237.
HOVERGENiHBG080113.
InParanoidiQ91WQ3.
KOiK01866.

Miscellaneous databases

ChiTaRSiYars. mouse.
NextBioi358652.
PROiQ91WQ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WQ3.
CleanExiMM_YARS.
ExpressionAtlasiQ91WQ3. baseline and differential.
GenevestigatoriQ91WQ3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR002307. Tyr-tRNA-ligase.
[Graphical view]
PfamiPF00579. tRNA-synt_1b. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiSYYC_MOUSE
AccessioniPrimary (citable) accession number: Q91WQ3
Secondary accession number(s): Q3TEC8
, Q3U9A1, Q3UTA7, Q8BVT2, Q8C183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.