Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P28668

- SYEP_DROME

UniProt

P28668 - SYEP_DROME

Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

Aats-glupro

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 sitei217 – 2171ATPBy similarity
    Binding sitei404 – 4041ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi438 – 4425ATPBy 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 binding Source: UniProtKB-KW

    GO - Biological processi

    1. glutamyl-tRNA aminoacylation Source: InterPro
    2. prolyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_214144. Cytosolic tRNA aminoacylation.

    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:Aats-glupro
    ORF Names:CG5394
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0005674. Aats-glupro.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17141714Bifunctional glutamate/proline--tRNA ligasePRO_0000119741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1110 – 11101Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP28668.
    PRIDEiP28668.

    Expressioni

    Gene expression databases

    BgeeiP28668.

    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.

    Protein-protein interaction databases

    BioGridi67770. 45 interactions.
    IntActiP28668. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP28668.
    SMRiP28668. Positions 195-688, 748-797, 816-872, 894-943, 973-1022, 1048-1096, 1217-1714.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini744 – 80057WHEP-TRS 1Add
    BLAST
    Domaini816 – 87257WHEP-TRS 2Add
    BLAST
    Domaini890 – 94657WHEP-TRS 3Add
    BLAST
    Domaini969 – 102557WHEP-TRS 4Add
    BLAST
    Domaini1044 – 110057WHEP-TRS 5Add
    BLAST
    Domaini1118 – 117457WHEP-TRS 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni170 – 754585Glutamate--tRNA ligaseAdd
    BLAST
    Regioni1207 – 1714508Proline--tRNA ligaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi209 – 22012"HIGH" regionAdd
    BLAST
    Motifi438 – 4425"KMSKS" region

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1174 – 11807Poly-Gly

    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 6 WHEP-TRS domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0442.
    GeneTreeiENSGT00750000118170.
    InParanoidiP28668.
    KOiK14163.
    OMAiVAMLHIK.
    OrthoDBiEOG754HNH.
    PhylomeDBiP28668.

    Family and domain databases

    Gene3Di1.10.1160.10. 1 hit.
    1.10.287.10. 6 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. 6 hits.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SMARTiSM00946. ProRS-C_1. 1 hit.
    SM00991. WHEP-TRS. 6 hits.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 6 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. 6 hits.
    PS51185. WHEP_TRS_2. 6 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P28668-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSIKLKANLN NPPISGLATA HLINGTVPVE IVWSKEETSL QFPDNRLLVC     50
    HSNNDVLRAL ARAAPDYKLY GETAIERTQI DHWLSFSLTC EDDISWALSF 100
    LDKSIAPVTY LVANKLTIAD FALFNEMHSR YEFLAAKGIP QHVQRWYDLI 150
    TAQPLIQKVL QSLPEDAKVK RSPQSSKEQT PAKTGERKQE GKFVDLPGAE 200
    MGKVVVRFPP EASGYLHIGH AKAALLNQYY ALAFQGTLIM RFDDTNPAKE 250
    TVEFENVILG DLEQLQIKPD VFTHTSNYFD LMLDYCVRLI KESKAYVDDT 300
    PPEQMKLERE QRVESANRSN SVEKNLSLWE EMVKGSEKGQ KYCVRAKIDM 350
    SSPNGCMRDP TIYRCKNEPH PRTGTKYKVY PTYDFACPIV DAIENVTHTL 400
    RTTEYHDRDD QFYWFIDALK LRKPYIWSYS RLNMTNTVLS KRKLTWFVDS 450
    GLVDGWDDPR FPTVRGIIRR GMTVEGLKEF IIAQGSSKSV VFMNWDKIWA 500
    FNKKVIDPIA PRYTALEKEK RVIVNVAGAK VERIQVSVHP KDESLGKKTV 550
    LLGPRIYIDY VDAEALKEGE NATFINWGNI LIRKVNKDAS GNITSVDAAL 600
    NLENKDFKKT LKLTWLAVED DPSAYPPTFC VYFDNIISKA VLGKDEDFKQ 650
    FIGHKTRDEV PMLGDPELKK CKKGDIIQLQ RRGFFKVDVA YAPPSGYTNV 700
    PSPIVLFSIP DGHTKDVPTS GLKVNAPDAK ATKKASSPVS SSGQASELDS 750
    QISQQGDLVR DLKSKKAAKD QIDVAVKKLL ALKADYKSAT GKDWKPGQTS 800
    ASSAPVPAAS SSSANDAVSV NASIVKQGDL VRDLKGKKAS KPEIDAAVKT 850
    LLELKAQYKT LTGQDWKPGT VPTTAAPSAS AAPSVGVNDS VAQILSQITA 900
    QGDKVRELKS AKADKATVDA AVKTLLSLKA DYKAATGSDW KPGTTAPAPA 950
    AAPVKVKQEK NPDPASVLTV NTLLNKIAQQ GDKIRQLKSA KSEKSLVEAE 1000
    VKLLLALKTD YKSLTGQEWK PGTVAPAPTT VNVIDLTGGD SGSDVGSVLS 1050
    KIQAQGDKIR KLKSEKAAKN VIDPEVKTLL ALKGEYKTLS GKDWTPDAKS 1100
    EPAVVKKEAS PVSMASPAKD ELTQEINAQG EKVRAAKGNK AAKEVIDAEV 1150
    AKLLALKAKY KEVTGTDFPV AGRGGGGGGG SAKKAPKEAQ PKPAKPVKKE 1200
    PAADASGAVK KQTRLGLEAT KEDNLPDWYS QVITKGEMIE YYDVSGCYIL 1250
    RQWSFAIWKA IKTWFDAEIT RMGVKECYFP IFVSKAVLEK EKTHIADFAP 1300
    EVAWVTKSGD SDLAEPIAVR PTSETVMYPA YAKWVQSYRD LPIRLNQWNN 1350
    VVRWEFKQPT PFLRTREFLW QEGHTAFADK EEAAKEVLDI LDLYALVYTH 1400
    LLAIPVVKGR KTEKEKFAGG DYTTTVEAFI SASGRAIQGA TSHHLGQNFS 1450
    KMFEIVYEDP ETQQKKYVYQ NSWGITTRTI GVMIMVHADN QGLVLPPHVA 1500
    CIQAIVVPCG ITVNTKDDER AQLLDACKAL EKRLVGGGVR CEGDYRDNYS 1550
    PGWKFNHWEL KGVPLRLEVG PKDLKAQQLV AVRRDTVEKI TIPLADVEKK 1600
    IPALLETIHE SMLNKAQEDM TSHTKKVTNW TDFCGFLEQK NILLAPFCGE 1650
    ISCEDKIKAD SARGEEAEPG APAMGAKSLC IPFDQPAPIA ASDKCINPSC 1700
    TNKPKFYTLF GRSY 1714
    Length:1,714
    Mass (Da):189,412
    Last modified:March 1, 2004 - v2
    Checksum:i3F8CF3DB128765A8
    GO
    Isoform B (identifier: P28668-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-718: Missing.
         719-732: TSGLKVNAPDAKAT → MLNYLACGSLSSTS

    Note: No experimental confirmation available.

    Show »
    Length:996
    Mass (Da):107,835
    Checksum:i0E0D298DF6D006C9
    GO

    Sequence cautioni

    The sequence AAN71400.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1065DKSIA → TSPLP(PubMed:1756734)Curated
    Sequence conflicti102 – 1065DKSIA → TSPLP(PubMed:9063462)Curated
    Sequence conflicti233 – 2342AF → VC(PubMed:1756734)Curated
    Sequence conflicti233 – 2342AF → VC(PubMed:9063462)Curated
    Sequence conflicti341 – 3455KYCVR → NTACA(PubMed:1756734)Curated
    Sequence conflicti341 – 3455KYCVR → NTACA(PubMed:9063462)Curated
    Sequence conflicti583 – 5831R → K(PubMed:1756734)Curated
    Sequence conflicti583 – 5831R → K(PubMed:9063462)Curated
    Sequence conflicti692 – 6921A → L(PubMed:1756734)Curated
    Sequence conflicti692 – 6921A → L(PubMed:9063462)Curated
    Sequence conflicti753 – 7531S → T(PubMed:1756734)Curated
    Sequence conflicti753 – 7531S → T(PubMed:9063462)Curated
    Sequence conflicti802 – 8021S → T(PubMed:1756734)Curated
    Sequence conflicti802 – 8021S → T(PubMed:9063462)Curated
    Sequence conflicti873 – 8731T → P(PubMed:1756734)Curated
    Sequence conflicti873 – 8731T → P(PubMed:9063462)Curated
    Sequence conflicti887 – 8871V → G(PubMed:1756734)Curated
    Sequence conflicti887 – 8871V → G(PubMed:9063462)Curated
    Sequence conflicti1035 – 10351D → G in AAN71400. (PubMed:12537569)Curated
    Sequence conflicti1202 – 12021Missing(PubMed:1756734)Curated
    Sequence conflicti1202 – 12021Missing(PubMed:9063462)Curated
    Sequence conflicti1461 – 14611E → EK(PubMed:1756734)Curated
    Sequence conflicti1461 – 14611E → EK(PubMed:9063462)Curated
    Sequence conflicti1587 – 15871V → G(PubMed:1756734)Curated
    Sequence conflicti1587 – 15871V → G(PubMed:9063462)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 718718Missing in isoform B. 1 PublicationVSP_009609Add
    BLAST
    Alternative sequencei719 – 73214TSGLK…DAKAT → MLNYLACGSLSSTS in isoform B. 1 PublicationVSP_009610Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74104 mRNA. Translation: AAA28594.1.
    U59923 Genomic DNA. Translation: AAC47469.1.
    AE014297 Genomic DNA. Translation: AAF56211.1.
    AE014297 Genomic DNA. Translation: AAN13964.1.
    AY058703 mRNA. Translation: AAL13932.1.
    BT001645 mRNA. Translation: AAN71400.1. Different initiation.
    PIRiS18644.
    RefSeqiNP_524471.2. NM_079747.3. [P28668-1]
    NP_732925.1. NM_170103.2. [P28668-2]
    UniGeneiDm.1304.

    Genome annotation databases

    EnsemblMetazoaiFBtr0084511; FBpp0083898; FBgn0005674. [P28668-1]
    GeneIDi42834.
    KEGGidme:Dmel_CG5394.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74104 mRNA. Translation: AAA28594.1 .
    U59923 Genomic DNA. Translation: AAC47469.1 .
    AE014297 Genomic DNA. Translation: AAF56211.1 .
    AE014297 Genomic DNA. Translation: AAN13964.1 .
    AY058703 mRNA. Translation: AAL13932.1 .
    BT001645 mRNA. Translation: AAN71400.1 . Different initiation.
    PIRi S18644.
    RefSeqi NP_524471.2. NM_079747.3. [P28668-1 ]
    NP_732925.1. NM_170103.2. [P28668-2 ]
    UniGenei Dm.1304.

    3D structure databases

    ProteinModelPortali P28668.
    SMRi P28668. Positions 195-688, 748-797, 816-872, 894-943, 973-1022, 1048-1096, 1217-1714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67770. 45 interactions.
    IntActi P28668. 2 interactions.

    Proteomic databases

    PaxDbi P28668.
    PRIDEi P28668.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0084511 ; FBpp0083898 ; FBgn0005674 . [P28668-1 ]
    GeneIDi 42834.
    KEGGi dme:Dmel_CG5394.

    Organism-specific databases

    CTDi 42834.
    FlyBasei FBgn0005674. Aats-glupro.

    Phylogenomic databases

    eggNOGi COG0442.
    GeneTreei ENSGT00750000118170.
    InParanoidi P28668.
    KOi K14163.
    OMAi VAMLHIK.
    OrthoDBi EOG754HNH.
    PhylomeDBi P28668.

    Enzyme and pathway databases

    Reactomei REACT_214144. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    GenomeRNAii 42834.
    NextBioi 830817.
    PROi P28668.

    Gene expression databases

    Bgeei P28668.

    Family and domain databases

    Gene3Di 1.10.1160.10. 1 hit.
    1.10.287.10. 6 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. 6 hits.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SMARTi SM00946. ProRS-C_1. 1 hit.
    SM00991. WHEP-TRS. 6 hits.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 6 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. 6 hits.
    PS51185. WHEP_TRS_2. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase."
      Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.
      EMBO J. 10:4267-4277(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    2. "Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex."
      Cerini C., Semeriva M., Gratecos D.
      Eur. J. Biochem. 244:176-185(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
      Strain: Oregon-R.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
      Strain: Berkeley.
      Tissue: Embryo.
    6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1110, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiSYEP_DROME
    AccessioniPrimary (citable) accession number: P28668
    Secondary accession number(s): Q8IGR4
    , Q8IMX9, Q95TL3, Q9VCF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3