P47897 (SYQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

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
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	1	1	Removed Ref.3
	Chain	2 – 775	774	Glutamine--tRNA ligase		PRO_0000195860
Regions
	Motif	270 – 280	11	"HIGH" region
	Motif	493 – 497	5	"KMSKS" region
Sites
	Binding site	496	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3 Ref.7
	Modified residue	70	1	Phosphoserine Ref.6
	Modified residue	309	1	N6-acetyllysine Ref.8
	Modified residue	491	1	Phosphotyrosine Ref.4 Ref.5
	Modified residue	620	1	N6-acetyllysine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P47897 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: ADDE23E6C442FF73	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

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: 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. , 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.
IPI	IPI00925046.
PIR	I37422.
RefSeq	NP_005042.1. NM_005051.1.
UniGene	Hs.79322.
3D structure databases
ProteinModelPortal	P47897.
SMR	P47897. Positions 249-771.
ModBase	Search...
Protein-protein interaction databases
IntAct	P47897. 8 interactions.
MINT	MINT-5004268.
STRING	P47897.
PTM databases
PhosphoSite	P47897.
Polymorphism databases
DMDM	1351170.
Proteomic databases
PRIDE	P47897.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000306125; ENSP00000307567; ENSG00000172053.
GeneID	5859.
KEGG	hsa:5859.
UCSC	uc003cvx.1. human.
Organism-specific databases
CTD	5859.
GeneCards	GC03M049108.
H-InvDB	HIX0022770.
HGNC	HGNC:9751. QARS.
HPA	HPA036986.
MIM	603727. gene.
neXtProt	NX_P47897.
PharmGKB	PA34093.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07482.
HOGENOM	HBG334108.
HOVERGEN	HBG000889.
InParanoid	P47897.
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
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]
Gene3D	G3DSA: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.
KO	K01886.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 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
DrugBank	DB00130. L-Glutamine.
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:	January 25, 2012
This is version 116 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.