AMPKBI5'-AMP-activated protein kinase beta subunit, interation domain
|SMART accession number:||SM01010|
|Description:||This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologues Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain is sometimes found in proteins belonging to this family.|
|Interpro abstract (IPR006828):|
Association with the SNF1 complex (ASC) domain is found in the Sip1/Sip2/Gal83/AMPKbeta subunits of the SNF1/AMP-activated protein kinase (AMPK) complex [(PUBMED:11252725)]. The SNF1/AMPK are heterotrimeric enzymes composed of a catalytic alpha-subunit, a regulatory gamma-subunit and a regulatory/targeting beta-subunit [(PUBMED:9121458)]. Saccharomyces cerevisiae encodes three beta-subunit genes, Sip1, Sip2 and Gal83 [(PUBMED:7813428), (PUBMED:10990457)]. The beta-subunits function as target selective adaptors that recruit the catalytic kinase and regulator Snf4/gamma-subunits. The ASC domain is required for interaction with Snf4 [(PUBMED:11252725), (PUBMED:9121458)].
The SNF1 kinase complex is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation [(PUBMED:17981722), (PUBMED:10207618)]. As glucose levels decrease, Snf1 is activated and promotes the use of alternative carbon sources.
|GO function:||protein binding (GO:0005515)|
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