Glutamine--tRNA ligase - Homo sapiens (Human)

Contribute

Send feedback

Read comments (?) or add your own

P47897 (SYQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamine--tRNA ligase
EC=6.1.1.18

Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS

Gene names

Name:

QARS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	775 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glutaminyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	ATP 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
PRRC2A	P48634	1	EBI-347462,EBI-347545

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 775

774

Glutamine--tRNA ligase

PRO_0000195860

Regions

Motif

270 – 280

"HIGH" region

Motif

493 – 497

"KMSKS" region

Sites

Binding site

496

ATP By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.3

Modified residue

Phosphoserine Ref.4

Modified residue

309

N6-acetyllysine Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P47897 [UniParc].

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

FASTA

775

87,799

        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' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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, MASS SPECTROMETRY.
[6]	"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] [Europe PMC] [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.
IPI	IPI00925046.
PIR	I37422.
RefSeq	NP_005042.1. NM_005051.2.
UniGene	Hs.79322.
3D structure databases
ProteinModelPortal	P47897.
ModBase	Search...
Protein-protein interaction databases
IntAct	P47897. 11 interactions.
MINT	MINT-5004268.
STRING	9606.ENSP00000307567.
PTM databases
PhosphoSite	P47897.
Polymorphism databases
DMDM	1351170.
Proteomic databases
PaxDb	P47897.
PRIDE	P47897.
Protocols and materials databases
DNASU	5859.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000306125; ENSP00000307567; ENSG00000172053.
GeneID	5859.
KEGG	hsa:5859.
UCSC	uc003cvx.3. human.
Organism-specific databases
CTD	5859.
GeneCards	GC03M049108.
HGNC	HGNC:9751. QARS.
HPA	HPA036986.
MIM	603727. gene.
neXtProt	NX_P47897.
PharmGKB	PA34093.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000259233.
HOVERGEN	HBG000889.
InParanoid	P47897.
KO	K01886.
OMA	RMPTIAG.
OrthoDB	EOG4ZKJKM.
PhylomeDB	P47897.
Enzyme and pathway databases
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P47897.
Bgee	P47897.
CleanEx	HS_QARS.
Genevestigator	P47897.
GermOnline	ENSG00000172053. Homo sapiens.
Family and domain databases
Gene3D	1.10.1160.10. 1 hit. 2.40.240.10. 2 hits. 3.40.50.620. 2 hits.
InterPro	IPR001412. 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]
PANTHER	PTHR10119. PTHR10119. 1 hit.
Pfam	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]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF50715. Ribosomal_L25rel. 1 hit.
TIGRFAMs	TIGR00440. glnS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P47897.
ChEMBL	CHEMBL3054.
ChiTaRS	QARS. human.
DrugBank	DB00130. L-Glutamine.
GenomeRNAi	5859.
NextBio	22754.
SOURCE	Search...

Entry information

Entry name

SYQ_HUMAN

Accession

Primary (citable) accession number: P47897

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents