Reviewed, UniProtKB/Swiss-Prot Q8CGC7 (SYEP_MOUSE)

Names and origin

Protein names

Recommended name:
    Bifunctional aminoacyl-tRNA synthetase
Including the following 2 domains:
    1- Recommended name:
            Glutamyl-tRNA synthetase
              EC=6.1.1.17
        Alternative name(s):
            Glutamate--tRNA ligase
    2- Recommended name:
            Prolyl-tRNA synthetase
              EC=6.1.1.15
        Alternative name(s):
            Proline--tRNA ligase

Gene names

Name:	Eprs
Synonyms:	Qprs

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA By similarity.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
Subunit structure	Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L By similarity.
Domain	The WHEP-TRS domain is involved in RNA binding By similarity.
Sequence similarities	In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family. In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family. Contains 3 WHEP-TRS domains.
Sequence caution	The sequence AAH40802.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Protein biosynthesis
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro prolyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
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 electronic annotation. Source: EC proline-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1512	1512	Bifunctional aminoacyl-tRNA synthetase		PRO_0000119744
Regions
	Domain	749 – 805	57	WHEP-TRS 1
	Domain	822 – 878	57	WHEP-TRS 2
	Domain	900 – 956	57	WHEP-TRS 3
	Nucleotide binding	432 – 436	5	ATP By similarity
	Region	164 – 759	596	Glutamyl-tRNA synthetase
	Region	760 – 956	197	3 X 57 AA approximate repeats
	Region	1007 – 1512	506	Prolyl-tRNA synthetase
	Motif	204 – 214	11	"HIGH" region
	Motif	432 – 436	5	"KMSKS" region
	Compositional bias	959 – 991	33	Asp/Glu/Lys-rich
Sites
	Binding site	211	1	ATP By similarity
	Binding site	398	1	ATP By similarity
Amino acid modifications
	Modified residue	300	1	N6-acetyllysine By similarity
	Modified residue	417	1	N6-acetyllysine By similarity
	Modified residue	498	1	N6-acetyllysine By similarity
	Modified residue	535	1	N6-acetyllysine By similarity
	Modified residue	542	1	N6-acetyllysine By similarity
	Modified residue	637	1	N6-acetyllysine By similarity
	Modified residue	788	1	N6-acetyllysine By similarity
	Modified residue	872	1	Phosphotyrosine By similarity
	Modified residue	883	1	Phosphoserine By similarity
	Modified residue	885	1	Phosphoserine By similarity
	Modified residue	1156	1	N6-acetyllysine By similarity
	Modified residue	1503	1	N6-acetyllysine By similarity
Natural variations
	Natural variant	871	1	D → E
Experimental info
	Sequence conflict	94	1	R → G in AAH40802. Ref.1
	Sequence conflict	172	1	N → S in AAH40802. Ref.1
	Sequence conflict	618	1	S → P in AAH40802. Ref.1
	Sequence conflict	986	1	G → R in X54327. Ref.3
	Sequence conflict	1141	1	A → P in AAH94679. Ref.1
	Sequence conflict	1290	1	N → S in AAH94679. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8CGC7-1 [UniParc]. Last modified December 4, 2007. Version 3. Checksum: 2440CBA306666000	FASTA	1,512	170,053
	10 20 30 40 50 60 MAALCLTVNA GNPPLEALLA VEHVKGDVSI SVEEGKENLL RVSETVAFTD VNSILRYLAR 70 80 90 100 110 120 IATTSGLYGT NLMEHTEIDH WLEFSATKLS SCDRLTSAIN ELNHCLSLRT YLVGNSLTLA 130 140 150 160 170 180 DLCVWATLKG SAAWQEHLKQ NKTLVHVKRW FGFLEAQQAF RSVGTKWDVS GNRATVAPDK 190 200 210 220 230 240 KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN 250 260 270 280 290 300 PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK 310 320 330 340 350 360 AEREQRTESK HRKNSVEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK 370 380 390 400 410 420 IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI 430 440 450 460 470 480 WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS 490 500 510 520 530 540 SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVVPVNV LDAQEEMKEV ARHPKNPDVG 550 560 570 580 590 600 LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD 610 620 630 640 650 660 YKKTTKITWL AESTHALSIP AVCVTYEHLI TKPVLGKDED FKQYINKDSK HEELMLGDPC 670 680 690 700 710 720 LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCREAPCILI YIPDGHTKEM PTSGSKEKTK 730 740 750 760 770 780 VEISKKETSS APKERPAPAV SSTCATAEDS SVLYSRVAVQ GDVVRELKAK KAPKEDIDAA 790 800 810 820 830 840 VKQLLTLKAE YKEKTGQEYK PGNPSAAAVQ TVSTKSSSNT VESTSLYNKV AAQGEVVRKL 850 860 870 880 890 900 KAEKAPKAKV TEAVECLLSL KAEYKEKTGK DYVPGQPPAS QNSHSNPVSN AQPAGAEKPE 910 920 930 940 950 960 AKVLFDRVAC QGEVVRKLKA EKASKDQVDS AVQELLQLKA QYKSLTGIEY KPVSATGAED 970 980 990 1000 1010 1020 KDKKKKEKEN KSEKQNKPQK QNDGQGKDSS KSQGSGLSSG GAGEGQGPKK QTRLGLEAKK 1030 1040 1050 1060 1070 1080 EENLAEWYSQ VITKSEMIEY YDVSGCYILR PWSYSIWESI KDFFDAEIKK LGVENCYFPI 1090 1100 1110 1120 1130 1140 FVSQAALEKE KNHIEDFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL 1150 1160 1170 1180 1190 1200 AVRLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATFE EAADEVLQIL ELYARVYEEL 1210 1220 1230 1240 1250 1260 LAIPVVRGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGAT SHHLGQNFSK MCEIVFEDPK 1270 1280 1290 1300 1310 1320 TPGEKQFAYQ CSWGLTTRTI GVMVMVHGDN MGLVLPPRVA SVQVVVIPCG ITNALSEEDR 1330 1340 1350 1360 1370 1380 EALMAKCNEY RRRLLGANIR VRVDLRDNYS PGWKFNHWEL KGVPVRLEVG PRDMKSCQFV 1390 1400 1410 1420 1430 1440 AVRRDTGEKL TIAEKEAEAK LEKVLEDIQL NLFTRASEDL KTHMVVSNTL EDFQKVLDAG 1450 1460 1470 1480 1490 1500 KVAQIPFCGE IDCEDWIKKM TARDQDVEPG APSMGAKSLC IPFNPLCELQ PGAMCVCGKN 1510 PAKFYTLFGR SY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Eye and Mammary tumor.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962. Strain: C57BL/6J. Tissue: Pancreas.
[3]	"M.musculus mRNA for glutamyl-tRNA synthetase." Knippers R. Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 406-1512.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC040802 mRNA. Translation: AAH40802.1. Sequence problems. BC094679 mRNA. Translation: AAH94679.1. AK148463 mRNA. Translation: BAE28568.1. X54327 mRNA. No translation available.
IPI	IPI00339916.
RefSeq	NP_084011.1.
UniGene	Mm.154511
3D structure databases
HSSP	HSSP built from PDB template 1FYJ based on UniProtKB P07814.
SMR	Q8CGC7. Positions 749-804, 826-875.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8CGC7.
PTM databases
PhosphoSite	Q8CGC7.
Proteomic databases
PRIDE	Q8CGC7.
Genome annotation databases
Ensembl	ENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615; Mus musculus. [Genome view]
GeneID	107508.
KEGG	mmu:107508.
UCSC	uc007dze.1. mouse. uc007dzg.1. mouse.
Organism-specific databases
CTD	107508.
MGI	MGI:97838. Eprs.
Phylogenomic databases
HOGENOM	Q8CGC7.
HOVERGEN	Q8CGC7.
Enzyme and pathway databases
BRENDA	6.1.1.15. 244. 6.1.1.17. 244.
Gene expression databases
ArrayExpress	Q8CGC7.
Bgee	Q8CGC7.
CleanEx	MM_EPRS.
Genevestigator	Q8CGC7.
GermOnline	ENSMUSG00000026615. Mus musculus.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR001412. aa-tRNA-synth_I_CS. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004154. Anticodon_bd. IPR004526. Glu-tRNA-synth_Ic_arc/euk. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom. IPR020059. Glu/Gln-tRNA-synth_Ic_codon-bd. IPR020060. Glu/Gln-tRNA-synth_Ic_N. IPR010987. Glutathione-S-Trfase_C-like. IPR004499. Pro-tRNA-synth_IIa_pro-type. IPR016061. Pro-tRNA_synth_II_C. IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl. IPR009068. S15_NS1_RNA_bd. IPR000738. WHEP-TRS. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 1 hit. G3DSA:2.40.240.10. Rbsml_L25/Gln-tRNA_synth_b-brl. 1 hit. G3DSA:1.10.287.10. S15_NS1_RNA_bd. 3 hits.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF09180. ProRS-C_1. 1 hit. PF00749. tRNA-synt_1c. 1 hit. PF03950. tRNA-synt_1c_C. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF00458. WHEP-TRS. 3 hits. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
TIGRFAMs	TIGR00463. gltX_arch. 1 hit. TIGR00408. proS_fam_I. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50862. AA_TRNA_LIGASE_II. 1 hit. PS00762. WHEP_TRS_1. 2 hits. PS51185. WHEP_TRS_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	358934.
SOURCE	Search...

Entry information

Entry name

SYEP_MOUSE

Accession

Primary (citable) accession number: Q8CGC7
Secondary accession number(s): Q3UFJ2, Q4VC16

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 4, 2007
Last modified:	October 13, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)