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P47897 (SYQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--tRNA ligase

EC=6.1.1.18
Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS
Gene names
Name:QARS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length775 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processglutaminyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Traceable author statement. Source: Reactome

mitochondrial matrix

Traceable author statement. Source: Reactome

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamine-tRNA ligase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRRC2AP486341EBI-347462,EBI-347545

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 775774Glutamine--tRNA ligase
PRO_0000195860

Regions

Motif270 – 28011"HIGH" region
Motif493 – 4975"KMSKS" region

Sites

Binding site4961ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.7
Modified residue701Phosphoserine Ref.6
Modified residue3091N6-acetyllysine Ref.8
Modified residue4911Phosphotyrosine Ref.4 Ref.5
Modified residue6201N6-acetyllysine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P47897 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: ADDE23E6C442FF73

FASTA77587,799
        10         20         30         40         50         60 
MAALDSLSLF TSLGLSEQKA RETLKNSALS AQLREAATQA QQTLGSTIDK ATGILLYGLA 

        70         80         90        100        110        120 
SRLRDTRRLS FLVSYIASKK IHTEPQLSAA LEYVRSHPLD PIDTVDFERE CGVGVIVTPE 

       130        140        150        160        170        180 
QIEEAVEAAI NRHRPQLLVE RYHFNMGLLM GEARAVLKWA DGKMIKNEVD MQVLHLLGPK 

       190        200        210        220        230        240 
LEADLEKKFK VAKARLEETD RRTAKDVVEN GETADQTLSL MEQLRGEALK FHKPGENYKT 

       250        260        270        280        290        300 
PGYVVTPHTM NLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL 

       310        320        330        340        350        360 
RFDDTNPEKE EAKFFTAICD MVAWLGYTPY KVTYASDYFD QLYAWAVELI RRGLAYVCHQ 

       370        380        390        400        410        420 
RGEELKGHNT LPSPWRDRPM EESLLLFEAM RKGKFSEGEA TLRMKLVMED GKMDPVAYRV 

       430        440        450        460        470        480 
KYTPHHRTGD KWCIYPTYDY THCLCDSIEH ITHSLCTKEF QARRSSYFWL CNALDVYCPV 

       490        500        510        520        530        540 
QWEYGRLNLH YAVVSKRKIL QLVATGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG 

       550        560        570        580        590        600 
VTVAQTTMEP HLLEACVRDV LNDTAPRAMA VLESLRVIIT NFPAAKSLDI QVPNFPADET 

       610        620        630        640        650        660 
KGFHQVPFAP IVFIERTDFK EEPEPGFKRL AWGQPVGLRH TGYVIELQHV VKGPSGCVES 

       670        680        690        700        710        720 
LEVTCRRADA GEKPKAFIHW VSQPLMCEVR LYERLFQHKN PEDPTEVPGG FLSDLNLASL 

       730        740        750        760        770 
HVVDAALVDC SVALAKPFDK FQFERLGYFS VDPDSHQGKL VFNRTVTLKE DPGKV 

« Hide

References

« Hide 'large scale' references
[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: 8078941] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain 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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung, Ovary and Placenta.
[3]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, MASS SPECTROMETRY.
Tissue: Hepatoma.
[4]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-491, MASS SPECTROMETRY.
[5]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-491, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, MASS SPECTROMETRY.
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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-309 AND LYS-620, MASS SPECTROMETRY.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76013 mRNA. Translation: CAA53600.1.
BC000394 mRNA. Translation: AAH00394.1.
BC001567 mRNA. Translation: AAH01567.1.
BC029739 mRNA. Translation: AAH29739.1.
IPIIPI00925046.
PIRI37422.
RefSeqNP_005042.1. NM_005051.1.
UniGeneHs.79322.

3D structure databases

ProteinModelPortalP47897.
SMRP47897. Positions 249-771.
ModBaseSearch...

Protein-protein interaction databases

IntActP47897. 8 interactions.
MINTMINT-5004268.
STRINGP47897.

PTM databases

PhosphoSiteP47897.

Polymorphism databases

DMDM1351170.

Proteomic databases

PRIDEP47897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306125; ENSP00000307567; ENSG00000172053.
GeneID5859.
KEGGhsa:5859.
UCSCuc003cvx.1. human.

Organism-specific databases

CTD5859.
GeneCardsGC03M049108.
H-InvDBHIX0022770.
HGNCHGNC:9751. QARS.
HPAHPA036986.
MIM603727. gene.
neXtProtNX_P47897.
PharmGKBPA34093.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07482.
HOGENOMHBG334108.
HOVERGENHBG000889.
InParanoidP47897.
OMARMPTIAG.
OrthoDBEOG4ZKJKM.
PhylomeDBP47897.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP47897.
BgeeP47897.
CleanExHS_QARS.
GenevestigatorP47897.
GermOnlineENSG00000172053. Homo sapiens.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ib.
IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:2.40.240.10. Rbsml_L25/Gln-tRNA_synth_b-brl. 2 hits.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01886.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. 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]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. Ribosomal_L25rel. 1 hit.
TIGRFAMsTIGR00440. GlnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00130. L-Glutamine.
NextBio22754.
SOURCESearch...

Entry information

Entry nameSYQ_HUMAN
AccessionPrimary (citable) accession number: P47897
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families