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Q9CXJ1

- SYEM_MOUSE

UniProt

Q9CXJ1 - SYEM_MOUSE

Protein

Probable glutamate--tRNA ligase, mitochondrial

Gene

Ears2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501ATPBy similarity
    Binding sitei76 – 761GlutamateBy similarity
    Binding sitei246 – 2461GlutamateBy similarity
    Binding sitei249 – 2491ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi284 – 2885ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate-tRNA(Gln) ligase activity Source: Ensembl
    3. glutamate-tRNA ligase activity Source: UniProtKB-EC
    4. tRNA binding Source: InterPro

    GO - Biological processi

    1. glutamyl-tRNA aminoacylation Source: Ensembl
    2. tRNA aminoacylation for mitochondrial protein translation Source: Ensembl

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glutamate--tRNA ligase, mitochondrial (EC:6.1.1.17)
    Alternative name(s):
    Glutamyl-tRNA synthetase
    Short name:
    GluRS
    Gene namesi
    Name:Ears2
    Synonyms:Kiaa1970
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1914667. Ears2.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4141MitochondrionSequence AnalysisAdd
    BLAST
    Chaini42 – 523482Probable glutamate--tRNA ligase, mitochondrialPRO_0000254562Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei256 – 2561N6-succinyllysine1 Publication
    Modified residuei486 – 4861N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9CXJ1.
    PRIDEiQ9CXJ1.

    PTM databases

    PhosphoSiteiQ9CXJ1.

    Expressioni

    Gene expression databases

    BgeeiQ9CXJ1.
    GenevestigatoriQ9CXJ1.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000033159.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CXJ1.
    SMRiQ9CXJ1. Positions 37-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 423Glutamate bindingBy similarity
    Regioni228 – 2325Glutamate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi45 – 539"HIGH" region
    Motifi284 – 2885"KMSKS" region

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0008.
    GeneTreeiENSGT00390000009759.
    HOGENOMiHOG000252720.
    HOVERGENiHBG056174.
    InParanoidiQ9CXJ1.
    KOiK01885.
    OMAiTKHSNVM.
    OrthoDBiEOG73Z2SZ.
    PhylomeDBiQ9CXJ1.
    TreeFamiTF313268.

    Family and domain databases

    Gene3Di1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00022_B. Glu_tRNA_synth_B.
    InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR004527. Glu-tRNA-ligase_bac/mito.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SUPFAMiSSF48163. SSF48163. 1 hit.
    TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9CXJ1-1 [UniParc]FASTAAdd to Basket

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    MAAPLKRLLL AEPHVVALGH RVGRREASLG PDPGAPVRVR FAPSPTGFLH    50
    LGGLRTALYN YIFAKKHQGS FILRLEDTDQ SRLVPGAAES IEDMLEWAGI 100
    PPDESPRRGG PAGPYCQSQR LALYAQATEA LLRSGAAYPC FCLPQRLELL 150
    KKEALRSRQT PRYDNRCRNL SQAQVAQKLA VDPKPAIRFR LEEAVPAFQD 200
    LVYGWTQHEV ASVEGDPVIL KSDGFPTYHL ACVVDDHHMS ISHVLRGSEW 250
    LVSTSKHLLL YQALGWQPPR FAHLPLLLNR DGSKLSKRQG DIFLEHFAAT 300
    GFLPEALLDI ITNCGSGFAE NQMGRTLPEL ITQFDLTRIT CHSALLDLEK 350
    LPEFNRLHLR RLVSSETQRP QLVEKLQGLV KEAFGSELQN KDVLDPAYME 400
    RILLLRQGHI SRLQDLVSPV YSYLWTRPAV HRSELGASSE NVDVIAKRLL 450
    GLLERPGLSL TQDVLNRELK KLSEGLEGAK HSSVMKLLRM ALSGQLQGPP 500
    VAEMMVSLGP KEVRERIQKV LSS 523
    Length:523
    Mass (Da):58,326
    Last modified:June 1, 2001 - v1
    Checksum:i39D506771FB96608
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881R → S in BAE39582. (PubMed:16141072)Curated
    Sequence conflicti227 – 2271T → A in BAE39582. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014324 mRNA. Translation: BAB29273.1.
    AK167506 mRNA. Translation: BAE39582.1.
    AK169225 mRNA. Translation: BAE40994.1.
    BC025907 mRNA. Translation: AAH25907.1.
    CCDSiCCDS21807.1.
    RefSeqiNP_080416.1. NM_026140.2.
    UniGeneiMm.45171.

    Genome annotation databases

    EnsembliENSMUST00000033159; ENSMUSP00000033159; ENSMUSG00000030871.
    GeneIDi67417.
    KEGGimmu:67417.
    UCSCiuc009joe.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014324 mRNA. Translation: BAB29273.1 .
    AK167506 mRNA. Translation: BAE39582.1 .
    AK169225 mRNA. Translation: BAE40994.1 .
    BC025907 mRNA. Translation: AAH25907.1 .
    CCDSi CCDS21807.1.
    RefSeqi NP_080416.1. NM_026140.2.
    UniGenei Mm.45171.

    3D structure databases

    ProteinModelPortali Q9CXJ1.
    SMRi Q9CXJ1. Positions 37-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000033159.

    Chemistry

    BindingDBi Q9CXJ1.

    PTM databases

    PhosphoSitei Q9CXJ1.

    Proteomic databases

    PaxDbi Q9CXJ1.
    PRIDEi Q9CXJ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033159 ; ENSMUSP00000033159 ; ENSMUSG00000030871 .
    GeneIDi 67417.
    KEGGi mmu:67417.
    UCSCi uc009joe.1. mouse.

    Organism-specific databases

    CTDi 124454.
    MGIi MGI:1914667. Ears2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0008.
    GeneTreei ENSGT00390000009759.
    HOGENOMi HOG000252720.
    HOVERGENi HBG056174.
    InParanoidi Q9CXJ1.
    KOi K01885.
    OMAi TKHSNVM.
    OrthoDBi EOG73Z2SZ.
    PhylomeDBi Q9CXJ1.
    TreeFami TF313268.

    Miscellaneous databases

    ChiTaRSi EARS2. mouse.
    NextBioi 324506.
    PROi Q9CXJ1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CXJ1.
    Genevestigatori Q9CXJ1.

    Family and domain databases

    Gene3Di 1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPi MF_00022_B. Glu_tRNA_synth_B.
    InterProi IPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR004527. Glu-tRNA-ligase_bac/mito.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF00749. tRNA-synt_1c. 1 hit.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SUPFAMi SSF48163. SSF48163. 1 hit.
    TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 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.
      Tissue: Head and Liver.
    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].
      Strain: FVB/N.
      Tissue: Kidney.
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSYEM_MOUSE
    AccessioniPrimary (citable) accession number: Q9CXJ1
    Secondary accession number(s): Q3TJB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 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