Relation Results

Summary

Name IARS1
Full Name Isoleucine--tRNA ligase, cytoplasmic
Synonyms Isoleucyl-tRNA synthetase, IRS, IleRS | IARS
Primary ID P41252
Links - -
Type protein
Relations 3
Function Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA- ...
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Type: Score: Layout: SPV 
0.20.20.2QRICH1IARS1ATF4Multiaminoacyl-tRNA synthetase

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Relations
Regulator
Mechanism
target
score ℹ
+ QRICH1up-regulates quantity by expression img/direct-activation.png transcriptional regulation IARS1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269406 Homo sapiens
pmid sentence
QRICH1 promotes the expression of translation-related genes. our combined ChIP-seq and RNA-seq analyses identified that QRICH1 and ATF4 were enriched at the promoters of these specific tRNA synthetases, and that ER stress positively regulated their transcription (Fig. 4I). Together, these findings suggest that QRICH1 and ATF4 modulate tRNA metabolic processes to promote secreted protein synthesis during ER stress.
Publications: 1 Organism: Homo Sapiens
+ ATF4up-regulates quantity by expression img/direct-activation.png transcriptional regulation IARS1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269427 Homo sapiens
pmid sentence
QRICH1 promotes the expression of translation-related genes. our combined ChIP-seq and RNA-seq analyses identified that QRICH1 and ATF4 were enriched at the promoters of these specific tRNA synthetases, and that ER stress positively regulated their transcription (Fig. 4I). Together, these findings suggest that QRICH1 and ATF4 modulate tRNA metabolic processes to promote secreted protein synthesis during ER stress.
Publications: 1 Organism: Homo Sapiens
+ IARS1form complex img/form-complex.png binding Multiaminoacyl-tRNA synthetase 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270354 Homo sapiens
pmid sentence
In mammalian cells, eight cytoplasmic aminoacyl-tRNA synthetases (AARS), and three non-synthetase proteins, reside in a large multi-tRNA synthetase complex (MSC). the MSC is suggested to be a super-complex of two identical, symmetrically arranged sub-units, each containing a single copy of the constituents, with the exception of LysRS which is present as a dimer in each sub-unit (Figure ​(Figure1B,1B, adapted from (27,28)). The sub-units are proposed to be joined by dimers of AspRS and the ProRS domain of GluProRS, and possibly by LysRS tetramers (20). Four AARSs containing GST-like domains important in protein-protein interactions form a MetRS-AIMP3–GluProRS–AIMP2 core of the complex (27,29). These proteins, together with AspRS, and possibly LeuRS and IleRS (30), form a distinct sub-complex denoted as sub-complex I (27). Sub-complex II consists of AIMP1, GlnRS, ArgRS, a dimer of LysRS, and AIMP2 (which is shared by both sub-complexes).
Publications: 1 Organism: Homo Sapiens
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