Relation Results

Summary

Name KARS1
Full Name Lysine--tRNA ligase
Synonyms Lysyl-tRNA synthetase, LysRS | KIAA0070
Primary ID Q15046
Links - -
Type protein
Relations 3
Function Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction

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Type: Score: Layout: SPV 
0.20.20.2MAPK3KARS1SOD1Multiaminoacyl-tRNA synthetase

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ up-regulates img/direct-activation.png phosphorylation KARS1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-186125 Ser207 PYEITLLsPCLHMLP Homo sapiens
pmid sentence
Lysrs serves as a key signaling molecule in the immune response by regulating gene expression. Lysrs was phosphorylated on serine 207 in a mapk-dependent manner, released from the multisynthetase complex, and translocated into the nucleus.
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity by destabilization img/direct_inhibition.png binding KARS1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-262800 Chlorocebus aethiops COS Cell
pmid sentence
In the presence of mutant SOD1, mitoKARS displays a high propensity to misfold and aggregate prior to its import into mitochondria, becoming a target for proteasome degradation.
Publications: 1 Organism: Chlorocebus Aethiops
+ form complex img/form-complex.png binding Multiaminoacyl-tRNA synthetase 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270353 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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