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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

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

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

GO - Biological processi

  1. brain development Source: UniProtKB
  2. gene expression Source: Reactome
  3. glutaminyl-tRNA aminoacylation Source: UniProtKB
  4. 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

Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Microcephaly, progressive, with seizures and cerebral and cerebellar atrophy (MSCCA) [MIM:615760]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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
VAR_071189
Natural varianti57 – 571Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
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
VAR_071191
Natural varianti515 – 5151R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 Publication
VAR_071192

Keywords - Diseasei

Disease mutation, Epilepsy, Primary microcephaly

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 775774Glutamine--tRNA ligasePRO_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

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.
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. Interacts with RARS.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111797. 96 interactions.
IntActiP47897. 34 interactions.
MINTiMINT-5004268.
STRINGi9606.ENSP00000307567.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3ZX-ray4.03C1-775[»]
ProteinModelPortaliP47897.
SMRiP47897. Positions 9-185, 231-774.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
GeneTreeiENSGT00550000074972.
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

        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
VAR_071189
Natural varianti57 – 571Y → H in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS. 1 Publication
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
VAR_071191
Natural varianti515 – 5151R → W in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; results in reduced protein solubility. 1 Publication
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.4. human. [P47897-1]
uc011bce.3. human.

Polymorphism databases

DMDMi1351170.

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 .
CCDSi CCDS2788.1. [P47897-1 ]
CCDS63633.1. [P47897-2 ]
PIRi I37422.
RefSeqi NP_001259002.1. NM_001272073.1. [P47897-2 ]
NP_005042.1. NM_005051.2. [P47897-1 ]
UniGenei Hs.79322.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4R3Z X-ray 4.03 C 1-775 [» ]
ProteinModelPortali P47897.
SMRi P47897. Positions 9-185, 231-774.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111797. 96 interactions.
IntActi P47897. 34 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 . [P47897-1 ]
ENST00000414533 ; ENSP00000390015 ; ENSG00000172053 . [P47897-2 ]
GeneIDi 5859.
KEGGi hsa:5859.
UCSCi uc003cvx.4. human. [P47897-1 ]
uc011bce.3. human.

Organism-specific databases

CTDi 5859.
GeneCardsi GC03M049108.
HGNCi HGNC:9751. QARS.
HPAi HPA036986.
MIMi 603727. gene.
615760. phenotype.
neXtProti NX_P47897.
Orphaneti 404437. Diffuse cerebral and cerebellar atrophy-intractable seizures-progressive microcephaly syndrome.
PharmGKBi PA34093.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0008.
GeneTreei ENSGT00550000074972.
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

Bgeei P47897.
CleanExi HS_QARS.
ExpressionAtlasi P47897. baseline and differential.
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].
  12. "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.

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: November 26, 2014
This is version 146 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

External Data

Dasty 3