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Protein

Probable glutamate--tRNA ligase, mitochondrial

Gene

Ears2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501ATPBy similarity
Binding sitei76 – 761GlutamateBy similarity
Binding sitei246 – 2461GlutamateBy similarity
Binding sitei249 – 2491ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi284 – 2885ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-tRNA(Gln) ligase activity Source: MGI
  3. glutamate-tRNA ligase activity Source: MGI
  4. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: MGI
  2. tRNA aminoacylation for mitochondrial protein translation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glutamate--tRNA ligase, mitochondrial (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:Ears2
Synonyms:Kiaa1970
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1914667. Ears2.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence AnalysisAdd
BLAST
Chaini42 – 523482Probable glutamate--tRNA ligase, mitochondrialPRO_0000254562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei256 – 2561N6-succinyllysine1 Publication
Modified residuei486 – 4861N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CXJ1.
PaxDbiQ9CXJ1.
PRIDEiQ9CXJ1.

PTM databases

PhosphoSiteiQ9CXJ1.

Expressioni

Gene expression databases

BgeeiQ9CXJ1.
GenevestigatoriQ9CXJ1.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033159.

Structurei

3D structure databases

ProteinModelPortaliQ9CXJ1.
SMRiQ9CXJ1. Positions 37-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 423Glutamate bindingBy similarity
Regioni228 – 2325Glutamate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 539"HIGH" region
Motifi284 – 2885"KMSKS" region

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0008.
GeneTreeiENSGT00390000009759.
HOGENOMiHOG000252720.
HOVERGENiHBG056174.
InParanoidiQ9CXJ1.
KOiK01885.
OMAiPAHSYLW.
OrthoDBiEOG73Z2SZ.
PhylomeDBiQ9CXJ1.
TreeFamiTF313268.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CXJ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPLKRLLL AEPHVVALGH RVGRREASLG PDPGAPVRVR FAPSPTGFLH
60 70 80 90 100
LGGLRTALYN YIFAKKHQGS FILRLEDTDQ SRLVPGAAES IEDMLEWAGI
110 120 130 140 150
PPDESPRRGG PAGPYCQSQR LALYAQATEA LLRSGAAYPC FCLPQRLELL
160 170 180 190 200
KKEALRSRQT PRYDNRCRNL SQAQVAQKLA VDPKPAIRFR LEEAVPAFQD
210 220 230 240 250
LVYGWTQHEV ASVEGDPVIL KSDGFPTYHL ACVVDDHHMS ISHVLRGSEW
260 270 280 290 300
LVSTSKHLLL YQALGWQPPR FAHLPLLLNR DGSKLSKRQG DIFLEHFAAT
310 320 330 340 350
GFLPEALLDI ITNCGSGFAE NQMGRTLPEL ITQFDLTRIT CHSALLDLEK
360 370 380 390 400
LPEFNRLHLR RLVSSETQRP QLVEKLQGLV KEAFGSELQN KDVLDPAYME
410 420 430 440 450
RILLLRQGHI SRLQDLVSPV YSYLWTRPAV HRSELGASSE NVDVIAKRLL
460 470 480 490 500
GLLERPGLSL TQDVLNRELK KLSEGLEGAK HSSVMKLLRM ALSGQLQGPP
510 520
VAEMMVSLGP KEVRERIQKV LSS
Length:523
Mass (Da):58,326
Last modified:June 1, 2001 - v1
Checksum:i39D506771FB96608
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881R → S in BAE39582. (PubMed:16141072)Curated
Sequence conflicti227 – 2271T → A in BAE39582. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014324 mRNA. Translation: BAB29273.1.
AK167506 mRNA. Translation: BAE39582.1.
AK169225 mRNA. Translation: BAE40994.1.
BC025907 mRNA. Translation: AAH25907.1.
CCDSiCCDS21807.1.
RefSeqiNP_080416.1. NM_026140.2.
UniGeneiMm.45171.

Genome annotation databases

EnsembliENSMUST00000033159; ENSMUSP00000033159; ENSMUSG00000030871.
GeneIDi67417.
KEGGimmu:67417.
UCSCiuc009joe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014324 mRNA. Translation: BAB29273.1.
AK167506 mRNA. Translation: BAE39582.1.
AK169225 mRNA. Translation: BAE40994.1.
BC025907 mRNA. Translation: AAH25907.1.
CCDSiCCDS21807.1.
RefSeqiNP_080416.1. NM_026140.2.
UniGeneiMm.45171.

3D structure databases

ProteinModelPortaliQ9CXJ1.
SMRiQ9CXJ1. Positions 37-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033159.

Chemistry

BindingDBiQ9CXJ1.

PTM databases

PhosphoSiteiQ9CXJ1.

Proteomic databases

MaxQBiQ9CXJ1.
PaxDbiQ9CXJ1.
PRIDEiQ9CXJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033159; ENSMUSP00000033159; ENSMUSG00000030871.
GeneIDi67417.
KEGGimmu:67417.
UCSCiuc009joe.1. mouse.

Organism-specific databases

CTDi124454.
MGIiMGI:1914667. Ears2.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0008.
GeneTreeiENSGT00390000009759.
HOGENOMiHOG000252720.
HOVERGENiHBG056174.
InParanoidiQ9CXJ1.
KOiK01885.
OMAiPAHSYLW.
OrthoDBiEOG73Z2SZ.
PhylomeDBiQ9CXJ1.
TreeFamiTF313268.

Miscellaneous databases

ChiTaRSiEars2. mouse.
NextBioi324506.
PROiQ9CXJ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXJ1.
GenevestigatoriQ9CXJ1.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSYEM_MOUSE
AccessioniPrimary (citable) accession number: Q9CXJ1
Secondary accession number(s): Q3TJB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.