MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organisation. The C-terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad []. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands [].
This entry represents the lysyl-tRNA synthetase (LysRS) binding domain of AIMP2 (aminoacyl tRNA synthase complex-interacting multifunctional protein 2). LysRS can serve as a transcription regulator that can be released from the cytoplasmic multi-tRNA synthetase complex (MSC) to activate the transcription factor MITF in stimulated mast cells. In quiescent cells, LysRS is held in the MSC via its interactions with AIMP2 [].
This is a thioredoxin like domain found in AIMP2 proteins (aminoacyl tRNA synthetase complex interacting multifunctional protein 2). AIMP2 is a component of human multi-tRNA synthetase complex (MSC). MSC is a macromolecular protein complex consisting of nine different ARSs and three ARS-interacting multifunctional proteins (AIMPs) [].
This family includes inner membrane proteins from plants and fungi, including Heh2/Src1 from budding yeasts and Lem2/Mug61 from fission yeasts [, , , ]. These proteins contain the N-terminal HEH/LEM domain that anchors the chromatin to the nuclear periphery, and a MSC (MAN1/Src1C-terminal) domain in their C-terminal region. They are involved in meiosis, required for the correct meiotic chromosome segregation.
Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (AIMP2), also known as multisynthase complex auxiliary component p38, is required for assembly and stability of the multi-tRNA synthetase complex (MSC complex) []. MSC is a macromolecular protein complex consisting of nine different ARSs and three ARS-interacting multifunctional proteins (AIMPs) [].
