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Reviewed, UniProtKB/Swiss-Prot Q5JPH6 (SYEM_HUMAN)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable glutamyl-tRNA synthetase, mitochondrial
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase
      Short name=GluRS
Gene names
Name: EARS2
Synonyms: KIAA1970
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion Potential
Chain42 – 523482Probable glutamyl-tRNA synthetase, mitochondrial
PRO_0000254560

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

Natural variations

Natural variant4571S → G: dbSNP rs6497671. Ref.1 Ref.2
VAR_028840

Sequences

Sequence LengthMass (Da)Tools
Q5JPH6-1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: FA9B19569AD9F5DB

FASTA52358,689
        10         20         30         40         50         60 
MAALLRRLLQ RERPSAASGR PVGRREANLG TDAGVAVRVR FAPSPTGFLH LGGLRTALYN 

        70         80         90        100        110        120 
YIFAKKYQGS FILRLEDTDQ TRVVPGAAEN IEDMLEWAGI PPDESPRRGG PAGPYQQSQR 

       130        140        150        160        170        180 
LELYAQATEA LLKTGAAYPC FCSPQRLELL KKEALRNHQT PRYDNRCRNM SQEQVAQKLA 

       190        200        210        220        230        240 
KDPKPAIRFR LEQVVPAFQD LVYGWNRHEV ASVEGDPVIM KSDGFPTYHL ACVVDDHHMG 

       250        260        270        280        290        300 
ISHVLRGSEW LVSTAKHLLL YQALGWQPPH FAHLPLLLNR DGSKLSKRQG DVFLEHFAAD 

       310        320        330        340        350        360 
GFLPDSLLDI ITNCGSGFAE NQMGRTLPEL ITQFNLTQVT CHSALLDLEK LPEFNRLHLQ 

       370        380        390        400        410        420 
RLVSNESQRR QLVGKLQVLV EEAFGCQLQN RDVLNPVYVE RILLLRQGHI CRLQDLVSPV 

       430        440        450        460        470        480 
YSYLWTRPAV GRAQLDAISE KVDVIAKRVL GLLERSSMSL TQDMLNGELK KLSEGLEGTK 

       490        500        510        520 
YSNVMKLLRM ALSGQQQGPP VAEMMLALGP KEVRERIQKV VSS 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-457.
Tissue: Kidney.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-457.
Tissue: Testis.
[3]"Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
Nagase T., Kikuno R., Ohara O.
DNA Res. 8:319-327(2001) [PubMed: 11853319] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-523.
Tissue: Brain.
[4]"Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS."
Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M.
Biochemistry 44:4805-4816(2005) [PubMed: 15779907] [Abstract]
Cited for: IDENTIFICATION.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AK095998 mRNA. Translation: BAG53194.1.
AL832489 mRNA. Translation: CAI46121.1.
AB075850 mRNA. Translation: BAB85556.1.
IPIIPI00642156.
RefSeqNP_001077083.1.
UniGeneHs.696113

3D structure databases

HSSPHSSP built from PDB template 1J09 based on UniProtKB P27000.
ModBaseSearch...

Genome annotation databases

EnsemblENSG00000103356. Homo sapiens. [Contig view]
GeneID124454.
KEGGhsa:124454.
NMPDRfig|9606.3.peg.11882.

Organism-specific databases

GeneCardsGC16M023440.
HGNCHGNC:29419. EARS2.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ5JPH6.
OMAQ5JPH6. RLELYAQ.

Enzyme and pathway databases

BRENDA6.1.1.17. 247.

Gene expression databases

ArrayExpressQ5JPH6.
BgeeQ5JPH6.
CleanExHS_EARS2.
GermOnlineENSG00000103356. Homo sapiens.

Family and domain databases

InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00142. L-Glutamic Acid.
NextBio81282.

Entry information

Entry nameSYEM_HUMAN
AccessionPrimary (citable) accession number: Q5JPH6
Secondary accession number(s): B3KTT2, Q8TF31
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: June 16, 2009
This is version 37 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents