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Q9CXJ1 (SYEM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

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

Names and origin

Protein namesRecommended name:
Probable glutamate--tRNA ligase, mitochondrial
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:Ears2
Synonyms:Kiaa1970
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 length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion Potential
Chain42 – 523482Probable glutamate--tRNA ligase, mitochondrial
PRO_0000254562

Regions

Nucleotide binding284 – 2885ATP By similarity
Region40 – 423Glutamate binding By similarity
Region228 – 2325Glutamate binding By similarity
Motif45 – 539"HIGH" region
Motif284 – 2885"KMSKS" region

Sites

Binding site501ATP By similarity
Binding site761Glutamate By similarity
Binding site2461Glutamate By similarity
Binding site2491ATP By similarity

Amino acid modifications

Modified residue4861N6-acetyllysine By similarity

Experimental info

Sequence conflict1881R → S in BAE39582. Ref.1
Sequence conflict2271T → A in BAE39582. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CXJ1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 39D506771FB96608

FASTA52358,326
        10         20         30         40         50         60 
MAAPLKRLLL AEPHVVALGH RVGRREASLG PDPGAPVRVR FAPSPTGFLH LGGLRTALYN 

        70         80         90        100        110        120 
YIFAKKHQGS FILRLEDTDQ SRLVPGAAES IEDMLEWAGI PPDESPRRGG PAGPYCQSQR 

       130        140        150        160        170        180 
LALYAQATEA LLRSGAAYPC FCLPQRLELL KKEALRSRQT PRYDNRCRNL SQAQVAQKLA 

       190        200        210        220        230        240 
VDPKPAIRFR LEEAVPAFQD LVYGWTQHEV ASVEGDPVIL KSDGFPTYHL ACVVDDHHMS 

       250        260        270        280        290        300 
ISHVLRGSEW LVSTSKHLLL YQALGWQPPR FAHLPLLLNR DGSKLSKRQG DIFLEHFAAT 

       310        320        330        340        350        360 
GFLPEALLDI ITNCGSGFAE NQMGRTLPEL ITQFDLTRIT CHSALLDLEK LPEFNRLHLR 

       370        380        390        400        410        420 
RLVSSETQRP QLVEKLQGLV KEAFGSELQN KDVLDPAYME RILLLRQGHI SRLQDLVSPV 

       430        440        450        460        470        480 
YSYLWTRPAV HRSELGASSE NVDVIAKRLL GLLERPGLSL TQDVLNRELK KLSEGLEGAK 

       490        500        510        520 
HSSVMKLLRM ALSGQLQGPP VAEMMVSLGP KEVRERIQKV LSS

« Hide

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: C57BL/6J.
Tissue: Head 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK014324 mRNA. Translation: BAB29273.1.
AK167506 mRNA. Translation: BAE39582.1.
AK169225 mRNA. Translation: BAE40994.1.
BC025907 mRNA. Translation: AAH25907.1.
IPIIPI00110380.
RefSeqNP_080416.1. NM_026140.2.
UniGeneMm.45171.

3D structure databases

HSSPHSSP built from PDB template 1NZJ based on UniProtKB P27305.
ProteinModelPortalQ9CXJ1.
SMRQ9CXJ1. Positions 37-499.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033159.

PTM databases

PhosphoSiteQ9CXJ1.

Proteomic databases

PaxDbQ9CXJ1.
PRIDEQ9CXJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033159; ENSMUSP00000033159; ENSMUSG00000030871.
GeneID67417.
KEGGmmu:67417.
UCSCuc009joe.1. mouse.

Organism-specific databases

CTD124454.
MGIMGI:1914667. Ears2.
RougeSearch...

Phylogenomic databases

eggNOGCOG0008.
GeneTreeENSGT00390000009759.
HOGENOMHOG000252720.
HOVERGENHBG056174.
InParanoidQ9CXJ1.
KOK01885.
OMAYESMELL.
OrthoDBEOG418BN8.

Gene expression databases

BgeeQ9CXJ1.
GenevestigatorQ9CXJ1.
GermOnlineENSMUSG00000030871. Mus musculus.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9CXJ1.
ChiTaRSEARS2. mouse.
NextBio324506.
SOURCESearch...

Entry information

Entry nameSYEM_MOUSE
AccessionPrimary (citable) accession number: Q9CXJ1
Secondary accession number(s): Q3TJB3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 93 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