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Q8CGC7

- SYEP_MOUSE

UniProt

Q8CGC7 - SYEP_MOUSE

Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

Eprs

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA By similarity. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.By similarity1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei211 – 2111ATPBy similarity
    Binding sitei398 – 3981ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi432 – 4365ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate-tRNA ligase activity Source: UniProtKB-EC
    3. proline-tRNA ligase activity Source: UniProtKB-EC
    4. RNA stem-loop binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to interferon-gamma Source: UniProtKB
    2. glutamyl-tRNA aminoacylation Source: InterPro
    3. negative regulation of translation Source: UniProtKB
    4. prolyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis, Translation regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional glutamate/proline--tRNA ligase
    Alternative name(s):
    Bifunctional aminoacyl-tRNA synthetase
    Including the following 2 domains:
    Glutamate--tRNA ligase (EC:6.1.1.17)
    Alternative name(s):
    Glutamyl-tRNA synthetase
    Short name:
    GluRS
    Proline--tRNA ligase (EC:6.1.1.15)
    Alternative name(s):
    Prolyl-tRNA synthetase
    Short name:
    ProRS
    Gene namesi
    Name:Eprs
    Synonyms:Qprs
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:97838. Eprs.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro
    2. GAIT complex Source: UniProtKB
    3. ribonucleoprotein complex Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi999 – 9991S → A: Not active in translation inhibition. 1 Publication
    Mutagenesisi999 – 9991S → D: Active in translation inhibition (phosphomimetic). 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15121512Bifunctional glutamate/proline--tRNA ligasePRO_0000119744Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei300 – 3001N6-acetyllysine; alternate1 Publication
    Modified residuei300 – 3001N6-malonyllysine; alternateBy similarity
    Modified residuei417 – 4171N6-acetyllysineBy similarity
    Modified residuei498 – 4981N6-acetyllysineBy similarity
    Modified residuei535 – 5351N6-acetyllysineBy similarity
    Modified residuei542 – 5421N6-acetyllysineBy similarity
    Modified residuei637 – 6371N6-acetyllysineBy similarity
    Modified residuei788 – 7881N6-acetyllysine1 Publication
    Modified residuei861 – 8611N6-acetyllysine1 Publication
    Modified residuei872 – 8721PhosphotyrosineBy similarity
    Modified residuei885 – 8851PhosphoserineBy similarity
    Modified residuei999 – 9991Phosphoserine1 Publication
    Modified residuei1503 – 15031N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated at Ser-999 in macrophages in a IFN-gamma-dependent manner; the phosphorylation is involving CDK5 and is causing release from the multisynthetase complex, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition. Phosphorylation at Ser-999 is specifically required for the interaction of GAIT complex-associated RPL13A with eIF4G By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8CGC7.
    PaxDbiQ8CGC7.
    PRIDEiQ8CGC7.

    PTM databases

    PhosphoSiteiQ8CGC7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8CGC7.
    BgeeiQ8CGC7.
    CleanExiMM_EPRS.
    GenevestigatoriQ8CGC7.

    Interactioni

    Subunit structurei

    Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L By similarity. Component of the GAIT complex.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi223350. 11 interactions.
    IntActiQ8CGC7. 3 interactions.
    MINTiMINT-1869828.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CGC7.
    SMRiQ8CGC7. Positions 749-804, 826-875, 900-952, 1016-1512.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini749 – 80557WHEP-TRS 1Add
    BLAST
    Domaini822 – 87857WHEP-TRS 2Add
    BLAST
    Domaini900 – 95657WHEP-TRS 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni164 – 759596Glutamate--tRNA ligaseAdd
    BLAST
    Regioni760 – 9561973 X 57 AA approximate repeatsAdd
    BLAST
    Regioni1007 – 1512506Proline--tRNA ligaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi204 – 21411"HIGH" regionAdd
    BLAST
    Motifi432 – 4365"KMSKS" region

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi959 – 99133Asp/Glu/Lys-richAdd
    BLAST

    Domaini

    The WHEP-TRS domain is involved in RNA binding.By similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family.Curated
    In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.Curated
    Contains 3 WHEP-TRS domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0442.
    GeneTreeiENSGT00550000074815.
    HOGENOMiHOG000022047.
    HOVERGENiHBG017875.
    InParanoidiQ8CGC7.
    KOiK14163.
    OMAiVAMLHIK.
    OrthoDBiEOG754HNH.
    TreeFamiTF300380.

    Family and domain databases

    Gene3Di1.10.1160.10. 1 hit.
    1.10.287.10. 3 hits.
    1.20.1050.10. 1 hit.
    2.40.240.10. 2 hits.
    3.30.110.30. 1 hit.
    3.40.50.620. 2 hits.
    3.40.50.800. 1 hit.
    HAMAPiMF_01571. Pro_tRNA_synth_type3.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR004526. Glu-tRNA-synth_arc/euk.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    IPR004499. Pro-tRNA-ligase_IIa_arc-type.
    IPR016061. Pro-tRNA_ligase_II_C.
    IPR017449. Pro-tRNA_synth_II.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009068. S15_NS1_RNA-bd.
    IPR000738. WHEP-TRS.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF14497. GST_C_3. 1 hit.
    PF03129. HGTP_anticodon. 1 hit.
    PF09180. ProRS-C_1. 1 hit.
    PF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF00458. WHEP-TRS. 3 hits.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SMARTiSM00946. ProRS-C_1. 1 hit.
    SM00991. WHEP-TRS. 3 hits.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 3 hits.
    SSF47616. SSF47616. 1 hit.
    SSF50715. SSF50715. 1 hit.
    SSF52954. SSF52954. 1 hit.
    SSF64586. SSF64586. 1 hit.
    TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
    TIGR00408. proS_fam_I. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    PS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS00762. WHEP_TRS_1. 2 hits.
    PS51185. WHEP_TRS_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8CGC7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALCLTVNA GNPPLEALLA VEHVKGDVSI SVEEGKENLL RVSETVAFTD     50
    VNSILRYLAR IATTSGLYGT NLMEHTEIDH WLEFSATKLS SCDRLTSAIN 100
    ELNHCLSLRT YLVGNSLTLA DLCVWATLKG SAAWQEHLKQ NKTLVHVKRW 150
    FGFLEAQQAF RSVGTKWDVS GNRATVAPDK KQDVGKFVEL PGAEMGKVTV 200
    RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK 250
    VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK 300
    AEREQRTESK HRKNSVEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC 350
    MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH 400
    DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW 450
    DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI 500
    DPVAPRYVAL LKKEVVPVNV LDAQEEMKEV ARHPKNPDVG LKPVWYSPKV 550
    FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD 600
    YKKTTKITWL AESTHALSIP AVCVTYEHLI TKPVLGKDED FKQYINKDSK 650
    HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCREAPCILI 700
    YIPDGHTKEM PTSGSKEKTK VEISKKETSS APKERPAPAV SSTCATAEDS 750
    SVLYSRVAVQ GDVVRELKAK KAPKEDIDAA VKQLLTLKAE YKEKTGQEYK 800
    PGNPSAAAVQ TVSTKSSSNT VESTSLYNKV AAQGEVVRKL KAEKAPKAKV 850
    TEAVECLLSL KAEYKEKTGK DYVPGQPPAS QNSHSNPVSN AQPAGAEKPE 900
    AKVLFDRVAC QGEVVRKLKA EKASKDQVDS AVQELLQLKA QYKSLTGIEY 950
    KPVSATGAED KDKKKKEKEN KSEKQNKPQK QNDGQGKDSS KSQGSGLSSG 1000
    GAGEGQGPKK QTRLGLEAKK EENLAEWYSQ VITKSEMIEY YDVSGCYILR 1050
    PWSYSIWESI KDFFDAEIKK LGVENCYFPI FVSQAALEKE KNHIEDFAPE 1100
    VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL PVRLNQWCNV 1150
    VRWEFKHPQP FLRTREFLWQ EGHSAFATFE EAADEVLQIL ELYARVYEEL 1200
    LAIPVVRGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGAT SHHLGQNFSK 1250
    MCEIVFEDPK TPGEKQFAYQ CSWGLTTRTI GVMVMVHGDN MGLVLPPRVA 1300
    SVQVVVIPCG ITNALSEEDR EALMAKCNEY RRRLLGANIR VRVDLRDNYS 1350
    PGWKFNHWEL KGVPVRLEVG PRDMKSCQFV AVRRDTGEKL TIAEKEAEAK 1400
    LEKVLEDIQL NLFTRASEDL KTHMVVSNTL EDFQKVLDAG KVAQIPFCGE 1450
    IDCEDWIKKM TARDQDVEPG APSMGAKSLC IPFNPLCELQ PGAMCVCGKN 1500
    PAKFYTLFGR SY 1512
    Length:1,512
    Mass (Da):170,079
    Last modified:July 27, 2011 - v4
    Checksum:iD14F6EA015B1BB6A
    GO

    Sequence cautioni

    The sequence AAH40802.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941R → G in AAH40802. (PubMed:15489334)Curated
    Sequence conflicti172 – 1721N → S in AAH40802. (PubMed:15489334)Curated
    Sequence conflicti618 – 6181S → P in AAH40802. (PubMed:15489334)Curated
    Sequence conflicti986 – 9861G → R in X54327. 1 PublicationCurated
    Sequence conflicti1290 – 12901N → S in AAH94679. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti871 – 8711D → E.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC129195 Genomic DNA. No translation available.
    AC131980 Genomic DNA. No translation available.
    BC040802 mRNA. Translation: AAH40802.1. Sequence problems.
    BC094679 mRNA. Translation: AAH94679.1.
    AK148463 mRNA. Translation: BAE28568.1.
    X54327 mRNA. No translation available.
    CCDSiCCDS35818.1.
    RefSeqiNP_084011.1. NM_029735.1.
    UniGeneiMm.154511.
    Mm.490980.

    Genome annotation databases

    EnsembliENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615.
    GeneIDi107508.
    KEGGimmu:107508.
    UCSCiuc007dze.1. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC129195 Genomic DNA. No translation available.
    AC131980 Genomic DNA. No translation available.
    BC040802 mRNA. Translation: AAH40802.1 . Sequence problems.
    BC094679 mRNA. Translation: AAH94679.1 .
    AK148463 mRNA. Translation: BAE28568.1 .
    X54327 mRNA. No translation available.
    CCDSi CCDS35818.1.
    RefSeqi NP_084011.1. NM_029735.1.
    UniGenei Mm.154511.
    Mm.490980.

    3D structure databases

    ProteinModelPortali Q8CGC7.
    SMRi Q8CGC7. Positions 749-804, 826-875, 900-952, 1016-1512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 223350. 11 interactions.
    IntActi Q8CGC7. 3 interactions.
    MINTi MINT-1869828.

    PTM databases

    PhosphoSitei Q8CGC7.

    Proteomic databases

    MaxQBi Q8CGC7.
    PaxDbi Q8CGC7.
    PRIDEi Q8CGC7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000046514 ; ENSMUSP00000045841 ; ENSMUSG00000026615 .
    GeneIDi 107508.
    KEGGi mmu:107508.
    UCSCi uc007dze.1. mouse.

    Organism-specific databases

    CTDi 2058.
    MGIi MGI:97838. Eprs.

    Phylogenomic databases

    eggNOGi COG0442.
    GeneTreei ENSGT00550000074815.
    HOGENOMi HOG000022047.
    HOVERGENi HBG017875.
    InParanoidi Q8CGC7.
    KOi K14163.
    OMAi VAMLHIK.
    OrthoDBi EOG754HNH.
    TreeFami TF300380.

    Miscellaneous databases

    NextBioi 358934.
    PROi Q8CGC7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CGC7.
    Bgeei Q8CGC7.
    CleanExi MM_EPRS.
    Genevestigatori Q8CGC7.

    Family and domain databases

    Gene3Di 1.10.1160.10. 1 hit.
    1.10.287.10. 3 hits.
    1.20.1050.10. 1 hit.
    2.40.240.10. 2 hits.
    3.30.110.30. 1 hit.
    3.40.50.620. 2 hits.
    3.40.50.800. 1 hit.
    HAMAPi MF_01571. Pro_tRNA_synth_type3.
    InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR004526. Glu-tRNA-synth_arc/euk.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    IPR004499. Pro-tRNA-ligase_IIa_arc-type.
    IPR016061. Pro-tRNA_ligase_II_C.
    IPR017449. Pro-tRNA_synth_II.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009068. S15_NS1_RNA-bd.
    IPR000738. WHEP-TRS.
    [Graphical view ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF14497. GST_C_3. 1 hit.
    PF03129. HGTP_anticodon. 1 hit.
    PF09180. ProRS-C_1. 1 hit.
    PF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF00458. WHEP-TRS. 3 hits.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SMARTi SM00946. ProRS-C_1. 1 hit.
    SM00991. WHEP-TRS. 3 hits.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 3 hits.
    SSF47616. SSF47616. 1 hit.
    SSF50715. SSF50715. 1 hit.
    SSF52954. SSF52954. 1 hit.
    SSF64586. SSF64586. 1 hit.
    TIGRFAMsi TIGR00463. gltX_arch. 1 hit.
    TIGR00408. proS_fam_I. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    PS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS00762. WHEP_TRS_1. 2 hits.
    PS51185. WHEP_TRS_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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: C57BL/6 and FVB/N.
      Tissue: Eye and Mammary tumor.
    3. "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] OF 1-962.
      Strain: C57BL/6J.
      Tissue: Pancreas.
    4. "M.musculus mRNA for glutamyl-tRNA synthetase."
      Knippers R.
      Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 406-1512.
    5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
      Arif A., Chatterjee P., Moodt R.A., Fox P.L.
      Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-999, SUBUNIT, RECONSTITUTION OF THE GAIT COMPLEX, MUTAGENESIS OF SER-999.
    7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-788 AND LYS-861, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSYEP_MOUSE
    AccessioniPrimary (citable) accession number: Q8CGC7
    Secondary accession number(s): E9QKC4, Q3UFJ2, Q4VC16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 104 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, 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