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Protein

Glutamine--tRNA ligase

Gene

QARS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • brain development Source: UniProtKB
  • glutaminyl-tRNA aminoacylation Source: UniProtKB
  • 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

ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-379726. Mitochondrial tRNA aminoacylation.

Protein family/group databases

MoonProtiP47897.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9751. QARS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Microcephaly, progressive, with seizures and cerebral and cerebellar atrophy (MSCCA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615760
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
Corresponds to variant rs587777331 [ dbSNP | Ensembl ].
VAR_071189
Natural varianti57 – 571Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
Corresponds to variant rs587777333 [ dbSNP | Ensembl ].
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
Corresponds to variant rs587777332 [ dbSNP | Ensembl ].
VAR_071191
Natural varianti515 – 5151R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 Publication
Corresponds to variant rs587777334 [ dbSNP | Ensembl ].
VAR_071192

Keywords - Diseasei

Disease mutation, Epilepsy, Primary microcephaly

Organism-specific databases

MalaCardsiQARS.
MIMi615760. phenotype.
Orphaneti404437. Diffuse cerebral and cerebellar atrophy-intractable seizures-progressive microcephaly syndrome.
PharmGKBiPA34093.

Chemistry

ChEMBLiCHEMBL3054.
DrugBankiDB00130. L-Glutamine.

Polymorphism and mutation databases

DMDMi1351170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 775774Glutamine--tRNA ligasePRO_0000195860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei70 – 701PhosphoserineCombined sources
Modified residuei309 – 3091N6-acetyllysineCombined sources
Modified residuei495 – 4951PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP47897.
MaxQBiP47897.
PaxDbiP47897.
PeptideAtlasiP47897.
PRIDEiP47897.

PTM databases

iPTMnetiP47897.
PhosphoSiteiP47897.
SwissPalmiP47897.

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

BgeeiP47897.
CleanExiHS_QARS.
ExpressionAtlasiP47897. baseline and differential.
GenevisibleiP47897. HS.

Organism-specific databases

HPAiHPA036986.
HPA036987.

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
AESQ081173EBI-347462,EBI-717810
DTX2Q86UW93EBI-10209725,EBI-740376
KLC3Q6P5973EBI-10209725,EBI-1643885
LZTS2Q9BRK43EBI-10209725,EBI-741037
TCF12Q990813EBI-347462,EBI-722877
TRAF4Q9BUZ43EBI-347462,EBI-3650647
TRIP13Q156453EBI-10209725,EBI-358993
VPS37BQ9H9H43EBI-10209725,EBI-4400866

Protein-protein interaction databases

BioGridi111797. 124 interactions.
IntActiP47897. 50 interactions.
MINTiMINT-5004268.
STRINGi9606.ENSP00000307567.

Chemistry

BindingDBiP47897.

Structurei

Secondary structure

1
775
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127Combined sources
Helixi17 – 259Combined sources
Helixi27 – 4216Combined sources
Turni43 – 453Combined sources
Helixi50 – 6213Combined sources
Helixi66 – 683Combined sources
Helixi69 – 779Combined sources
Helixi84 – 9411Combined sources
Helixi104 – 1107Combined sources
Helixi119 – 14022Combined sources
Helixi141 – 1433Combined sources
Helixi147 – 1548Combined sources
Helixi162 – 17716Combined sources
Helixi220 – 2234Combined sources
Helixi226 – 2294Combined sources
Helixi237 – 2393Combined sources
Helixi249 – 26012Combined sources
Beta strandi265 – 2684Combined sources
Helixi278 – 29316Combined sources
Beta strandi297 – 3026Combined sources
Helixi312 – 32413Combined sources
Beta strandi330 – 3345Combined sources
Helixi335 – 3384Combined sources
Helixi339 – 35113Combined sources
Beta strandi354 – 3585Combined sources
Turni374 – 3774Combined sources
Helixi380 – 39112Combined sources
Beta strandi401 – 4044Combined sources
Beta strandi416 – 4205Combined sources
Turni426 – 4283Combined sources
Beta strandi433 – 4364Combined sources
Helixi438 – 44811Combined sources
Beta strandi452 – 4576Combined sources
Helixi464 – 47310Combined sources
Beta strandi480 – 4845Combined sources
Beta strandi487 – 4893Combined sources
Helixi496 – 5049Combined sources
Beta strandi507 – 5104Combined sources
Helixi519 – 5246Combined sources
Helixi529 – 53911Combined sources
Beta strandi546 – 5483Combined sources
Helixi551 – 56414Combined sources
Beta strandi570 – 5767Combined sources
Beta strandi578 – 5814Combined sources
Beta strandi592 – 5943Combined sources
Helixi599 – 6013Combined sources
Beta strandi603 – 6064Combined sources
Beta strandi613 – 6153Combined sources
Turni616 – 6183Combined sources
Beta strandi647 – 6504Combined sources
Beta strandi654 – 6563Combined sources
Beta strandi661 – 6633Combined sources
Beta strandi681 – 6833Combined sources
Beta strandi685 – 6928Combined sources
Beta strandi695 – 7006Combined sources
Turni702 – 7054Combined sources
Turni711 – 7144Combined sources
Beta strandi720 – 7223Combined sources
Beta strandi725 – 7284Combined sources
Beta strandi732 – 7343Combined sources
Beta strandi740 – 7434Combined sources
Turni744 – 7463Combined sources
Beta strandi747 – 7515Combined sources
Beta strandi757 – 7593Combined sources
Beta strandi761 – 7666Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3ZX-ray4.03C1-775[»]
4YE6X-ray2.40A1-775[»]
4YE8X-ray3.30A1-775[»]
4YE9X-ray2.70A1-775[»]
ProteinModelPortaliP47897.
SMRiP47897. Positions 9-185, 220-771.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1148. Eukaryota.
COG0008. LUCA.
GeneTreeiENSGT00550000074972.
HOGENOMiHOG000259233.
HOVERGENiHBG000889.
InParanoidiP47897.
KOiK01886.
OMAiEHEYHAS.
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]
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. AlignAdd to basket

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

        10         20         30         40         50
MAALDSLSLF TSLGLSEQKA RETLKNSALS AQLREAATQA QQTLGSTIDK
60 70 80 90 100
ATGILLYGLA SRLRDTRRLS FLVSYIASKK IHTEPQLSAA LEYVRSHPLD
110 120 130 140 150
PIDTVDFERE CGVGVIVTPE QIEEAVEAAI NRHRPQLLVE RYHFNMGLLM
160 170 180 190 200
GEARAVLKWA DGKMIKNEVD MQVLHLLGPK LEADLEKKFK VAKARLEETD
210 220 230 240 250
RRTAKDVVEN GETADQTLSL MEQLRGEALK FHKPGENYKT PGYVVTPHTM
260 270 280 290 300
NLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL
310 320 330 340 350
RFDDTNPEKE EAKFFTAICD MVAWLGYTPY KVTYASDYFD QLYAWAVELI
360 370 380 390 400
RRGLAYVCHQ RGEELKGHNT LPSPWRDRPM EESLLLFEAM RKGKFSEGEA
410 420 430 440 450
TLRMKLVMED GKMDPVAYRV KYTPHHRTGD KWCIYPTYDY THCLCDSIEH
460 470 480 490 500
ITHSLCTKEF QARRSSYFWL CNALDVYCPV QWEYGRLNLH YAVVSKRKIL
510 520 530 540 550
QLVATGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG VTVAQTTMEP
560 570 580 590 600
HLLEACVRDV LNDTAPRAMA VLESLRVIIT NFPAAKSLDI QVPNFPADET
610 620 630 640 650
KGFHQVPFAP IVFIERTDFK EEPEPGFKRL AWGQPVGLRH TGYVIELQHV
660 670 680 690 700
VKGPSGCVES LEVTCRRADA GEKPKAFIHW VSQPLMCEVR LYERLFQHKN
710 720 730 740 750
PEDPTEVPGG FLSDLNLASL HVVDAALVDC SVALAKPFDK FQFERLGYFS
760 770
VDPDSHQGKL VFNRTVTLKE DPGKV
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
Corresponds to variant rs587777331 [ dbSNP | Ensembl ].
VAR_071189
Natural varianti57 – 571Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
Corresponds to variant rs587777333 [ dbSNP | Ensembl ].
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
Corresponds to variant rs587777332 [ dbSNP | Ensembl ].
VAR_071191
Natural varianti515 – 5151R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 Publication
Corresponds to variant rs587777334 [ dbSNP | Ensembl ].
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:
EMBLi
GenBanki
DDBJi
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. [P47897-2]
NP_005042.1. NM_005051.2. [P47897-1]
UniGeneiHs.79322.

Genome annotation databases

EnsembliENST00000306125; ENSP00000307567; ENSG00000172053. [P47897-1]
ENST00000414533; ENSP00000390015; ENSG00000172053. [P47897-2]
GeneIDi5859.
KEGGihsa:5859.
UCSCiuc003cvx.5. human. [P47897-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P47897-2]
NP_005042.1. NM_005051.2. [P47897-1]
UniGeneiHs.79322.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3ZX-ray4.03C1-775[»]
4YE6X-ray2.40A1-775[»]
4YE8X-ray3.30A1-775[»]
4YE9X-ray2.70A1-775[»]
ProteinModelPortaliP47897.
SMRiP47897. Positions 9-185, 220-771.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111797. 124 interactions.
IntActiP47897. 50 interactions.
MINTiMINT-5004268.
STRINGi9606.ENSP00000307567.

Chemistry

BindingDBiP47897.
ChEMBLiCHEMBL3054.
DrugBankiDB00130. L-Glutamine.

Protein family/group databases

MoonProtiP47897.

PTM databases

iPTMnetiP47897.
PhosphoSiteiP47897.
SwissPalmiP47897.

Polymorphism and mutation databases

DMDMi1351170.

Proteomic databases

EPDiP47897.
MaxQBiP47897.
PaxDbiP47897.
PeptideAtlasiP47897.
PRIDEiP47897.

Protocols and materials databases

DNASUi5859.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306125; ENSP00000307567; ENSG00000172053. [P47897-1]
ENST00000414533; ENSP00000390015; ENSG00000172053. [P47897-2]
GeneIDi5859.
KEGGihsa:5859.
UCSCiuc003cvx.5. human. [P47897-1]

Organism-specific databases

CTDi5859.
GeneCardsiQARS.
HGNCiHGNC:9751. QARS.
HPAiHPA036986.
HPA036987.
MalaCardsiQARS.
MIMi603727. gene.
615760. phenotype.
neXtProtiNX_P47897.
Orphaneti404437. Diffuse cerebral and cerebellar atrophy-intractable seizures-progressive microcephaly syndrome.
PharmGKBiPA34093.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1148. Eukaryota.
COG0008. LUCA.
GeneTreeiENSGT00550000074972.
HOGENOMiHOG000259233.
HOVERGENiHBG000889.
InParanoidiP47897.
KOiK01886.
OMAiEHEYHAS.
OrthoDBiEOG75XGK9.
PhylomeDBiP47897.
TreeFamiTF105683.

Enzyme and pathway databases

ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-379726. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

ChiTaRSiQARS. human.
GeneWikiiQARS.
GenomeRNAii5859.
PROiP47897.
SOURCEiSearch...

Gene expression databases

BgeeiP47897.
CleanExiHS_QARS.
ExpressionAtlasiP47897. baseline and differential.
GenevisibleiP47897. HS.

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]
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]
ProtoNetiSearch...

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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  13. "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.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 6, 2016
This is version 164 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.