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P47897

- SYQ_HUMAN

UniProt

P47897 - SYQ_HUMAN

Protein

Glutamine--tRNA ligase

Gene

QARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Plays a critical role in brain development.1 Publication

    Catalytic activityi

    ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei496 – 4961ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamine-tRNA ligase activity Source: Reactome

    GO - Biological processi

    1. gene expression Source: Reactome
    2. glutaminyl-tRNA aminoacylation Source: InterPro
    3. tRNA aminoacylation for protein translation Source: Reactome

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.
    REACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine--tRNA ligase (EC:6.1.1.18)
    Alternative name(s):
    Glutaminyl-tRNA synthetase
    Short name:
    GlnRS
    Gene namesi
    Name:QARS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9751. QARS.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Microcephaly, progressive, with seizures and cerebral and cerebellar atrophy (MSCCA) [MIM:615760]: A severe, autosomal recessive, neurodevelopmental and neurodegenerative disorder characterized by progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, resulting in profoundly delayed development and hypotonia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451G → V in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
    VAR_071189
    Natural varianti57 – 571Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
    VAR_071190
    Natural varianti403 – 4031R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; does not interact with RARS; results in reduced protein solubility. 1 Publication
    VAR_071191
    Natural varianti515 – 5151R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 Publication
    VAR_071192

    Keywords - Diseasei

    Disease mutation, Epilepsy, Primary microcephaly

    Organism-specific databases

    MIMi615760. phenotype.
    PharmGKBiPA34093.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 775774Glutamine--tRNA ligasePRO_0000195860Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei70 – 701Phosphoserine1 Publication
    Modified residuei309 – 3091N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP47897.
    PaxDbiP47897.
    PRIDEiP47897.

    PTM databases

    PhosphoSiteiP47897.

    Expressioni

    Tissue specificityi

    Highly expressed in fetal cerebral cortex, particularly in the ventricular zone, inner subventricular zone, outer subventricular zone, and cortical plate.1 Publication

    Gene expression databases

    ArrayExpressiP47897.
    BgeeiP47897.
    CleanExiHS_QARS.
    GenevestigatoriP47897.

    Organism-specific databases

    HPAiHPA036986.

    Interactioni

    Subunit structurei

    Part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. Interacts with RARS.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRRC2AP486341EBI-347462,EBI-347545

    Protein-protein interaction databases

    BioGridi111797. 93 interactions.
    IntActiP47897. 34 interactions.
    MINTiMINT-5004268.
    STRINGi9606.ENSP00000307567.

    Structurei

    3D structure databases

    ProteinModelPortaliP47897.
    SMRiP47897. Positions 9-185, 231-774.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi270 – 28011"HIGH" regionAdd
    BLAST
    Motifi493 – 4975"KMSKS" region

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000259233.
    HOVERGENiHBG000889.
    InParanoidiP47897.
    KOiK01886.
    OMAiRMQKRAK.
    OrthoDBiEOG75XGK9.
    PhylomeDBiP47897.
    TreeFamiTF105683.

    Family and domain databases

    Gene3Di1.10.1160.10. 1 hit.
    2.40.240.10. 2 hits.
    3.40.50.620. 2 hits.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR004514. Gln-tRNA-synth.
    IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
    IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
    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.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    PF04558. tRNA_synt_1c_R1. 1 hit.
    PF04557. tRNA_synt_1c_R2. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SUPFAMiSSF50715. SSF50715. 1 hit.
    TIGRFAMsiTIGR00440. glnS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P47897-1) [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

    MAALDSLSLF TSLGLSEQKA RETLKNSALS AQLREAATQA QQTLGSTIDK    50
    ATGILLYGLA SRLRDTRRLS FLVSYIASKK IHTEPQLSAA LEYVRSHPLD 100
    PIDTVDFERE CGVGVIVTPE QIEEAVEAAI NRHRPQLLVE RYHFNMGLLM 150
    GEARAVLKWA DGKMIKNEVD MQVLHLLGPK LEADLEKKFK VAKARLEETD 200
    RRTAKDVVEN GETADQTLSL MEQLRGEALK FHKPGENYKT PGYVVTPHTM 250
    NLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL 300
    RFDDTNPEKE EAKFFTAICD MVAWLGYTPY KVTYASDYFD QLYAWAVELI 350
    RRGLAYVCHQ RGEELKGHNT LPSPWRDRPM EESLLLFEAM RKGKFSEGEA 400
    TLRMKLVMED GKMDPVAYRV KYTPHHRTGD KWCIYPTYDY THCLCDSIEH 450
    ITHSLCTKEF QARRSSYFWL CNALDVYCPV QWEYGRLNLH YAVVSKRKIL 500
    QLVATGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG VTVAQTTMEP 550
    HLLEACVRDV LNDTAPRAMA VLESLRVIIT NFPAAKSLDI QVPNFPADET 600
    KGFHQVPFAP IVFIERTDFK EEPEPGFKRL AWGQPVGLRH TGYVIELQHV 650
    VKGPSGCVES LEVTCRRADA GEKPKAFIHW VSQPLMCEVR LYERLFQHKN 700
    PEDPTEVPGG FLSDLNLASL HVVDAALVDC SVALAKPFDK FQFERLGYFS 750
    VDPDSHQGKL VFNRTVTLKE DPGKV 775
    Length:775
    Mass (Da):87,799
    Last modified:February 1, 1996 - v1
    Checksum:iADDE23E6C442FF73
    GO
    Isoform 2 (identifier: P47897-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         78-89: SKKIHTEPQLSA → T

    Show »
    Length:764
    Mass (Da):86,579
    Checksum:iBA9B1C92EE0C2F72
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451G → V in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
    VAR_071189
    Natural varianti57 – 571Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
    VAR_071190
    Natural varianti403 – 4031R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; does not interact with RARS; results in reduced protein solubility. 1 Publication
    VAR_071191
    Natural varianti515 – 5151R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 Publication
    VAR_071192

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei78 – 8912SKKIH…PQLSA → T in isoform 2. 1 PublicationVSP_055107Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76013 mRNA. Translation: CAA53600.1.
    AK301559 mRNA. Translation: BAG63054.1.
    AC135506 Genomic DNA. No translation available.
    BC000394 mRNA. Translation: AAH00394.1.
    BC001567 mRNA. Translation: AAH01567.1.
    BC029739 mRNA. Translation: AAH29739.1.
    CCDSiCCDS2788.1. [P47897-1]
    CCDS63633.1. [P47897-2]
    PIRiI37422.
    RefSeqiNP_001259002.1. NM_001272073.1.
    NP_005042.1. NM_005051.2.
    UniGeneiHs.79322.

    Genome annotation databases

    EnsembliENST00000306125; ENSP00000307567; ENSG00000172053. [P47897-1]
    ENST00000414533; ENSP00000390015; ENSG00000172053. [P47897-2]
    GeneIDi5859.
    KEGGihsa:5859.
    UCSCiuc003cvx.4. human. [P47897-1]

    Polymorphism databases

    DMDMi1351170.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76013 mRNA. Translation: CAA53600.1 .
    AK301559 mRNA. Translation: BAG63054.1 .
    AC135506 Genomic DNA. No translation available.
    BC000394 mRNA. Translation: AAH00394.1 .
    BC001567 mRNA. Translation: AAH01567.1 .
    BC029739 mRNA. Translation: AAH29739.1 .
    CCDSi CCDS2788.1. [P47897-1 ]
    CCDS63633.1. [P47897-2 ]
    PIRi I37422.
    RefSeqi NP_001259002.1. NM_001272073.1.
    NP_005042.1. NM_005051.2.
    UniGenei Hs.79322.

    3D structure databases

    ProteinModelPortali P47897.
    SMRi P47897. Positions 9-185, 231-774.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111797. 93 interactions.
    IntActi P47897. 34 interactions.
    MINTi MINT-5004268.
    STRINGi 9606.ENSP00000307567.

    Chemistry

    BindingDBi P47897.
    ChEMBLi CHEMBL3054.
    DrugBanki DB00130. L-Glutamine.

    PTM databases

    PhosphoSitei P47897.

    Polymorphism databases

    DMDMi 1351170.

    Proteomic databases

    MaxQBi P47897.
    PaxDbi P47897.
    PRIDEi P47897.

    Protocols and materials databases

    DNASUi 5859.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306125 ; ENSP00000307567 ; ENSG00000172053 . [P47897-1 ]
    ENST00000414533 ; ENSP00000390015 ; ENSG00000172053 . [P47897-2 ]
    GeneIDi 5859.
    KEGGi hsa:5859.
    UCSCi uc003cvx.4. human. [P47897-1 ]

    Organism-specific databases

    CTDi 5859.
    GeneCardsi GC03M049108.
    HGNCi HGNC:9751. QARS.
    HPAi HPA036986.
    MIMi 603727. gene.
    615760. phenotype.
    neXtProti NX_P47897.
    PharmGKBi PA34093.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000259233.
    HOVERGENi HBG000889.
    InParanoidi P47897.
    KOi K01886.
    OMAi RMQKRAK.
    OrthoDBi EOG75XGK9.
    PhylomeDBi P47897.
    TreeFami TF105683.

    Enzyme and pathway databases

    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.
    REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi QARS. human.
    GeneWikii QARS.
    GenomeRNAii 5859.
    NextBioi 22754.
    PROi P47897.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47897.
    Bgeei P47897.
    CleanExi HS_QARS.
    Genevestigatori P47897.

    Family and domain databases

    Gene3Di 1.10.1160.10. 1 hit.
    2.40.240.10. 2 hits.
    3.40.50.620. 2 hits.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR004514. Gln-tRNA-synth.
    IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
    IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
    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.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    PF04558. tRNA_synt_1c_R1. 1 hit.
    PF04557. tRNA_synt_1c_R2. 1 hit.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SUPFAMi SSF50715. SSF50715. 1 hit.
    TIGRFAMsi TIGR00440. glnS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer."
      Lamour V., Quevillon S., Diriong S., N'Guyen V.C., Lipinski M., Mirande M.
      Proc. Natl. Acad. Sci. U.S.A. 91:8670-8674(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain and Liver.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Mammary gland.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Lung, Ovary and Placenta.
    5. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-19; 206-225; 377-391 AND 602-616, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures."
      Zhang X., Ling J., Barcia G., Jing L., Wu J., Barry B.J., Mochida G.H., Hill R.S., Weimer J.M., Stein Q., Poduri A., Partlow J.N., Ville D., Dulac O., Yu T.W., Lam A.T., Servattalab S., Rodriguez J.
      , Boddaert N., Munnich A., Colleaux L., Zon L.I., Soll D., Walsh C.A., Nabbout R.
      Am. J. Hum. Genet. 94:547-558(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH RARS, VARIANTS MSCCA VAL-45; HIS-57; TRP-403 AND TRP-515, CHARACTERIZATION OF VARIANTS MSCCA VAL-45; HIS-57; TRP-403 AND TRP-515.

    Entry informationi

    Entry nameiSYQ_HUMAN
    AccessioniPrimary (citable) accession number: P47897
    Secondary accession number(s): B4DWJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3