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Q91WQ3

- SYYC_MOUSE

UniProt

Q91WQ3 - SYYC_MOUSE

Protein

Tyrosine--tRNA ligase, cytoplasmic

Gene

Yars

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. tRNA binding Source: UniProtKB-KW
    3. tyrosine-tRNA ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. tyrosyl-tRNA aminoacylation Source: InterPro

    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: Chromosome 4

    Organism-specific databases

    MGIiMGI:2147627. Yars.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: Ensembl

    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

    ArrayExpressiQ91WQ3.
    BgeeiQ91WQ3.
    CleanExiMM_YARS.
    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.
    GeneTreeiENSGT00750000117748.
    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

    MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKVYW GTATTGKPHV    50
    AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRTSYYENV 100
    IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDAKKAGA 150
    EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGVDQRK IFTFAEKYLP 200
    ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC 250
    EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT VYLELEKDFA 300
    AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPP 350
    AKGPAKNSEP EEVIPSRLDI RVGKILSVEK HPDADSLYVE KIDVGEAEPR 400
    TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVDSQGML LCASVEGVSR 450
    QVEPLDPPAG SAPGERVFVQ GYEKGQPDEE LKPKKKVFEK LQADFKISEE 500
    CIAQWKQTNF MTKLGFVSCK SLKGGNIS 528
    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:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENSMUST00000001365; ENSMUSP00000001365; ENSMUSG00000028811.
    GeneIDi107271.
    KEGGimmu:107271.
    UCSCiuc008uwk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_598912.4. NM_134151.4.
    UniGenei Mm.145488.

    3D structure databases

    ProteinModelPortali Q91WQ3.
    SMRi Q91WQ3. Positions 4-342, 360-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 223230. 1 interaction.
    IntActi Q91WQ3. 2 interactions.
    MINTi MINT-1855454.

    PTM databases

    PhosphoSitei Q91WQ3.

    Proteomic databases

    MaxQBi Q91WQ3.
    PaxDbi Q91WQ3.
    PRIDEi Q91WQ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001365 ; ENSMUSP00000001365 ; ENSMUSG00000028811 .
    GeneIDi 107271.
    KEGGi mmu:107271.
    UCSCi uc008uwk.2. mouse.

    Organism-specific databases

    CTDi 8565.
    MGIi MGI:2147627. Yars.

    Phylogenomic databases

    eggNOGi COG0162.
    GeneTreei ENSGT00750000117748.
    HOGENOMi HOG000228237.
    HOVERGENi HBG080113.
    InParanoidi Q91WQ3.
    KOi K01866.

    Miscellaneous databases

    NextBioi 358652.
    PROi Q91WQ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91WQ3.
    Bgeei Q91WQ3.
    CleanExi MM_YARS.
    Genevestigatori Q91WQ3.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    3.40.50.620. 1 hit.
    InterProi IPR002305. 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 ]
    Pfami PF00579. tRNA-synt_1b. 1 hit.
    PF01588. tRNA_bind. 1 hit.
    [Graphical view ]
    PRINTSi PR01040. TRNASYNTHTYR.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00234. tyrS. 1 hit.
    PROSITEi PS50886. TRBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 107 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