Q5JPH6 (SYEM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Protein biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from direct assay. Source: UniProtKB tRNA aminoacylation for mitochondrial protein translation Inferred from direct assay. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from direct assay. Source: UniProtKB glutamate-tRNA(Gln) ligase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 41	41	Mitochondrion Potential
	Chain	42 – 523	482	Probable glutamate--tRNA ligase, mitochondrial		PRO_0000254560
Regions
	Nucleotide binding	284 – 288	5	ATP By similarity
	Region	40 – 42	3	Glutamate binding By similarity
	Region	228 – 232	5	Glutamate binding By similarity
	Motif	45 – 53	9	"HIGH" region
	Motif	284 – 288	5	"KMSKS" region
Sites
	Binding site	50	1	ATP By similarity
	Binding site	76	1	Glutamate By similarity
	Binding site	246	1	Glutamate By similarity
	Binding site	249	1	ATP By similarity
Amino acid modifications
	Modified residue	486	1	N6-acetyllysine Ref.6
Natural variations
	Natural variant	457	1	S → G. Ref.1 Ref.2 Corresponds to variant rs6497671 [ dbSNP | Ensembl ].		VAR_028840

Sequences

	Sequence		Length	Mass (Da)
	Q5JPH6 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: FA9B19569AD9F5DB	FASTA	523	58,689
	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

References

	« Hide 'large scale' referencesShow '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. , 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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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.
[5]	"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.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, MASS SPECTROMETRY.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK095998 mRNA. Translation: BAG53194.1. AL832489 mRNA. Translation: CAI46121.1. CH471145 Genomic DNA. Translation: EAW55822.1. CH471145 Genomic DNA. Translation: EAW55824.1. AB075850 mRNA. Translation: BAB85556.1.
IPI	IPI00642156.
RefSeq	NP_001077083.1. NM_001083614.1.
UniGene	Hs.620541.
3D structure databases
HSSP	HSSP built from PDB template 1NZJ based on UniProtKB P27305.
ProteinModelPortal	Q5JPH6.
SMR	Q5JPH6. Positions 37-522.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5JPH6.
PTM databases
PhosphoSite	Q5JPH6.
Polymorphism databases
DMDM	117949790.
Proteomic databases
PRIDE	Q5JPH6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341597; ENSP00000343488; ENSG00000103356. ENST00000449606; ENSP00000395196; ENSG00000103356.
GeneID	124454.
KEGG	hsa:124454.
NMPDR	fig|9606.3.peg.11882.
UCSC	uc002dlt.2. human.
Organism-specific databases
CTD	124454.
GeneCards	GC16M023533.
HGNC	HGNC:29419. EARS2.
HPA	HPA043289. HPA043633.
MIM	612799. gene.
neXtProt	NX_Q5JPH6.
PharmGKB	PA144596439.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07186.
GeneTree	ENSGT00390000009759.
HOVERGEN	HBG056174.
InParanoid	Q5JPH6.
OrthoDB	EOG418BN8.
PhylomeDB	Q5JPH6.
Enzyme and pathway databases
Reactome	REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q5JPH6.
Bgee	Q5JPH6.
CleanEx	HS_EARS2.
Genevestigator	Q5JPH6.
GermOnline	ENSG00000103356. Homo sapiens.
Family and domain databases
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_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]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. GltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00142. L-Glutamic Acid.
NextBio	81282.
SOURCE	Search...

Entry information

Entry name

SYEM_HUMAN

Accession

Primary (citable) accession number: Q5JPH6
Secondary accession number(s): B3KTT2, D3DWF1, Q8TF31

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	January 25, 2012
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.