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Q9CZD3 (SYG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine--tRNA ligase
EC=6.1.1.14
Alternative name(s):
Diadenosine tetraphosphate synthetase
Short name=AP-4-A synthetase
Glycyl-tRNA synthetase
Short name=GlyRS
Gene names
Name:Gars
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs By similarity.

Catalytic activity

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity. Mitochondrion By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Contains 1 WHEP-TRS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Glycine--tRNA ligase
PRO_0000072999

Regions

Domain53 – 10957WHEP-TRS
Nucleotide binding321 – 3233ATP By similarity
Nucleotide binding331 – 3366ATP By similarity
Nucleotide binding447 – 4482ATP By similarity
Nucleotide binding570 – 5734ATP By similarity
Region336 – 3405Substrate binding By similarity
Region566 – 5705Substrate binding By similarity

Sites

Binding site2031Substrate By similarity
Binding site2891Substrate By similarity
Binding site4251Substrate By similarity
Binding site4251Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue1941N6-acetyllysine By similarity
Modified residue4431Phosphotyrosine Ref.4
Modified residue4911N6-acetyllysine By similarity

Experimental info

Sequence conflict51L → V in BAE38417. Ref.1
Sequence conflict5841H → N in BAE27003. Ref.1
Sequence conflict5971F → L in BAE27003. Ref.1
Sequence conflict6941N → S in AAH21747. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9CZD3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 596613F746B9C7D0

FASTA72981,878
        10         20         30         40         50         60 
MPCLLPSLLR ATRAALPLLS PPRVVAASAS QRLLSAPAQP AASRSSMDSA EELLAPLRLA 

        70         80         90        100        110        120 
VRQQGDFVRK LKEDKAPQVD VDRAVAELKA RKRVLEAKEL ALQPKDDIVD RAKMEDTLKR 

       130        140        150        160        170        180 
RFFYDQAFAI YGGVSGLYDF GPVGCALKNN IIQAWRQHFI QEEQILEIDC TMLTPEPVLK 

       190        200        210        220        230        240 
TSGHVDKFAD FMVKDVKNGE CFRADHLLKA HLQKLMSDKK CSAEKKSEME SVLAQLDNYG 

       250        260        270        280        290        300 
QQELADLFVN YNVKSPTTGN DLSPPVPFNL MFQTFIGPGG NMPGYLRPET AQGIFLNFKR 

       310        320        330        340        350        360 
LLEFNQGKLP FAAAQIGNSF RNEISPRSGL IRVREFTMAE IEHFVDPTEK DHPKFQSVAD 

       370        380        390        400        410        420 
LCLYLYSAKA QVTGQSARKM RLGDAVEQGV INNSVLGYFI GRIYLYLTKV GISPDKLRFR 

       430        440        450        460        470        480 
QHMENEMAHY ACDCWDAESK TSYGWIEIVG CADRSCYDLS CHARATKVPL VAEKPLKEPK 

       490        500        510        520        530        540 
TVNVVQFEPN KGAVGKAYKK DAKLVLEYLS ACDECYISEM ELLLSEKGEF TIETEGKTFQ 

       550        560        570        580        590        600 
LTKDMVSVKR FQKTLHVEEV VPSVIEPSFG LGRIMYTILE HTFHVREGDE QRTFFSFPAV 

       610        620        630        640        650        660 
VAPFKCSVLP LSQNQEFMPF VKELSEALTR NGVSHKVDDS SGSIGRRYAR TDEIGVAFGI 

       670        680        690        700        710        720 
TIDFDTVNKT PHTATLRDRD SMRQIRAEVS ELPNVVRDLA NGNITWADVE ARYPLFEGQE 


TGKKETVEE

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c and C57BL/6J.
Tissue: Embryo and Lung.
[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: Salivary gland.
[3]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 309-321; 554-573 AND 593-605, MASS SPECTROMETRY.
Tissue: Hippocampus.
[4]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-443, MASS SPECTROMETRY.
Tissue: Mast cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK146238 mRNA. Translation: BAE27003.1.
AK165857 mRNA. Translation: BAE38417.1.
BC021747 mRNA. Translation: AAH21747.1.
IPIIPI00112555.
RefSeqNP_851009.2. NM_180678.3.
UniGeneMm.250004.

3D structure databases

ProteinModelPortalQ9CZD3.
SMRQ9CZD3. Positions 119-193, 261-492, 556-717.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1856268.

PTM databases

PhosphoSiteQ9CZD3.

2D gel databases

REPRODUCTION-2DPAGEQ9CZD3.

Proteomic databases

PaxDbQ9CZD3.
PRIDEQ9CZD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003572; ENSMUSP00000003572; ENSMUSG00000029777.
GeneID353172.
KEGGmmu:353172.
UCSCuc009cai.1. mouse.

Organism-specific databases

CTD2617.
MGIMGI:2449057. Gars.

Phylogenomic databases

eggNOGCOG0423.
GeneTreeENSGT00390000016949.
HOGENOMHOG000242015.
HOVERGENHBG036190.
InParanoidQ9CZD3.
KOK01880.
OMAVFIASGH.
OrthoDBEOG4RV2QV.

Gene expression databases

BgeeQ9CZD3.
CleanExMM_GARS.
GenevestigatorQ9CZD3.
GermOnlineENSMUSG00000029777. Mus musculus.

Family and domain databases

Gene3D1.10.287.10. 1 hit.
3.40.50.800. 1 hit.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR009068. S15_NS1_RNA-bd.
IPR002315. tRNA-synt_gly.
IPR000738. WHEP-TRS.
[Graphical view]
PANTHERPTHR10745. PTHR10745. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view]
PRINTSPR01043. TRNASYNTHGLY.
SMARTSM00991. WHEP-TRS. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
TIGRFAMsTIGR00389. glyS_dimeric. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGARS. mouse.
NextBio400323.
SOURCESearch...

Entry information

Entry nameSYG_MOUSE
AccessionPrimary (citable) accession number: Q9CZD3
Secondary accession number(s): Q3TMM4, Q3UK01, Q8VC67
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: June 1, 2001
Last modified: May 29, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents