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P47897

- SYQ_HUMAN

UniProt

P47897 - SYQ_HUMAN

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Protein
Glutamine--tRNA ligase
Gene
QARS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

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

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34093.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 775774Glutamine--tRNA ligase
PRO_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

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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111797. 93 interactions.
IntActiP47897. 33 interactions.
MINTiMINT-5004268.
STRINGi9606.ENSP00000307567.

Structurei

3D structure databases

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

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi270 – 28011"HIGH" region
Add
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei78 – 8912SKKIH…PQLSA → T in isoform 2.
VSP_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]
PIRiI37422.
RefSeqiNP_001259002.1. NM_001272073.1.
NP_005042.1. NM_005051.2.
UniGeneiHs.79322.

Genome annotation databases

EnsembliENST00000306125; ENSP00000307567; ENSG00000172053.
ENST00000414533; ENSP00000390015; ENSG00000172053.
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 ]
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. 33 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 .
ENST00000414533 ; ENSP00000390015 ; ENSG00000172053 .
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.
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

« Hide 'large scale' publications
  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].

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: September 3, 2014
This is version 143 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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