Literature summary for 2.5.1.6 extracted from

Reytor, E.; Perez-Miguelsanz, J.; Alvarez, L.; Perez-Sala, D.; Pajares, M.A.
Conformational signals in the C-terminal domain of methionine adenosyltransferase I/III determine its nucleocytoplasmic distribution (2009), FASEB J., 23, 3347-3360.

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Protein Variants

Protein Variants	Comment	Organism
F251D	inactive, but displays correct nuclear localization and matrix binding	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasm	isoform MAT I, presence of two partially overlapping areas at the C-terminal end of the protein involved both in cytoplasmic retention and nuclear localization	Rattus norvegicus	5737	-
nucleus	isoform MAT I, in extrahepatic tissues, the protein colocalizes with nuclear matrix markers. Presence of two partially overlapping areas at the C-terminal end of the protein involved both in cytoplasmic retention and nuclear localization. Neither nuclear localization nor matrix binding requires activity. Nuclear accumulation of the active enzyme only correlates with histone H3K27 trimethylation among the epigenetic modifications evaluated	Rattus norvegicus	5634	-

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Subunits

Subunits	Comment	Organism
monomer	in nuclear fractions, presence of active tetramers and monomers	Rattus norvegicus
tetramer	in nuclear fractions, presence of active tetramers and monomers	Rattus norvegicus

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Release 2023.1 (January 2023)