Eprs1
entrez
107508
canonical
uniprot
Q8CGC7
canonical
ensembl
ENSMUSG00000026615
resolver
ensp
ENSMUSP00000045841
resolver
ensp
ENSMUSP00000277052
resolver
ensp
ENSMUSP00000277068
resolver
enst
ENSMUST00000046514
resolver
genesymbol
Eprs1
resolver
genesymbol_syn
Eprs
resolver
genesymbol_syn
Qprs
resolver
uniprot
E9QKC4
resolver
uniprot
Q3UFJ2
resolver
uniprot
Q4VC16
resolver
uniprot_entry
SYEP_MOUSE
resolver
uniprot_sec
E9QKC4
resolver
uniprot_sec
Q3UFJ2
resolver
uniprot_sec
Q4VC16
resolver
amino_acid_sequence
MAALCLTVNAGNPPLEALLAVEHVKGDVSISVEEGKENLLRVSETVAFTDVNSILRYLARIATTSGLYGTNLMEHTEIDHWLEFSATKLSSCDRLTSAINELNHCLSLRTYLVGNSLTLADLCVWATLKGSAAWQEHLKQNKTLVHVKRWFGFLEAQQAFRSVGTKWDVSGNRATVAPDKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRTESKHRKNSVEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVVPVNVLDAQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNINITKIHKNADGKITSLDAKLNLENKDYKKTTKITWLAESTHALSIPAVCVTYEHLITKPVLGKDEDFKQYINKDSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCREAPCILIYIPDGHTKEMPTSGSKEKTKVEISKKETSSAPKERPAPAVSSTCATAEDSSVLYSRVAVQGDVVRELKAKKAPKEDIDAAVKQLLTLKAEYKEKTGQEYKPGNPSAAAVQTVSTKSSSNTVESTSLYNKVAAQGEVVRKLKAEKAPKAKVTEAVECLLSLKAEYKEKTGKDYVPGQPPASQNSHSNPVSNAQPAGAEKPEAKVLFDRVACQGEVVRKLKAEKASKDQVDSAVQELLQLKAQYKSLTGIEYKPVSATGAEDKDKKKKEKENKSEKQNKPQKQNDGQGKDSSKSQGSGLSSGGAGEGQGPKKQTRLGLEAKKEENLAEWYSQVITKSEMIEYYDVSGCYILRPWSYSIWESIKDFFDAEIKKLGVENCYFPIFVSQAALEKEKNHIEDFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPVRLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATFEEAADEVLQILELYARVYEELLAIPVVRGRKTEKEKFAGGDYTTTIEAFISASGRAIQGATSHHLGQNFSKMCEIVFEDPKTPGEKQFAYQCSWGLTTRTIGVMVMVHGDNMGLVLPPRVASVQVVVIPCGITNALSEEDREALMAKCNEYRRRLLGANIRVRVDLRDNYSPGWKFNHWELKGVPVRLEVGPRDMKSCQFVAVRRDTGEKLTIAEKEAEAKLEKVLEDIQLNLFTRASEDLKTHMVVSNTLEDFQKVLDAGKVAQIPFCGEIDCEDWIKKMTARDQDVEPGAPSMGAKSLCIPFNPLCELQPGAMCVCGKNPAKFYTLFGRSY
uniprot
proteins
ec_number
6.1.1.15
uniprot
proteins
ec_number
6.1.1.17
uniprot
proteins
function
FUNCTION: Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (By similarity). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239). {ECO:0000250|UniProtKB:P07814, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:28178239}.
uniprot
proteins
mass_dalton
170079
uniprot
proteins
mutagenesis
MUTAGEN 999; /note="S->A: Loss of function in translation inhibition. Loss of interaction with SLC27A1. Mutant mice have no apparent developmental defect but display reduced adiposity associated with decreased insulin levels and adipocytes size. They also display increased lipolysis and fatty acid beta-oxidation and an extended lifespan. Adipocytes display decreased insulin-stimulated long-chain fatty acid uptake."; /evidence="ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:28178239"; MUTAGEN 999; /note="S->D: Constitutively active in translation inhibition (phosphomimetic). Mutant mice have no apparent developmental defect and do not display overt phenotype related to adiposity or lifespan."; /evidence="ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:28178239
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-999 by RPS6KB1; triggers EPRS1 release from the aminoacyl-tRNA synthetase multienzyme complex. In monocytes, the IFN-gamma-induced phosphorylation at Ser-999 releases EPRS1 from the aminoacyl-tRNA synthetase multienzyme complex, allowing its association with the GAIT complex. Phosphorylation at Ser-999 is specifically required for the RPL13A-mediated interaction of the GAIT complex with eIF4G (By similarity). Phosphorylation at Ser-999 by RPS6KB1, is also induced by insulin through activation of the mTORC1 signaling pathway and promotes the interaction of EPRS1 with SLC27A1 (PubMed:28178239). {ECO:0000250|UniProtKB:P07814, ECO:0000269|PubMed:28178239}.
uniprot
proteins
protein_family
Class-I aminoacyl-tRNA synthetase family
uniprot
proteins
protein_family
Glutamate--tRNA ligase type 2 subfamily; Class-II aminoacyl-tRNA synthetase family
uniprot
proteins
pubmed
12060739
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23071094
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
28178239
uniprot
proteins
sequence_length
1512
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P07814}. Membrane {ECO:0000269|PubMed:28178239}; Peripheral membrane protein {ECO:0000305|PubMed:28178239}. Note=Translocates from cytosol to membranes upon phosphorylation at Ser-999. {ECO:0000305|PubMed:28178239}.
uniprot
proteins