2QLV

Crystal structure of the heterotrimer core of the S. cerevisiae AMPK homolog SNF1

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000166	molecular_function	nucleotide binding
C	0004679	molecular_function	AMP-activated protein kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005641	cellular_component	nuclear envelope lumen
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006110	biological_process	regulation of glycolytic process
C	0006351	biological_process	DNA-templated transcription
C	0006357	biological_process	regulation of transcription by RNA polymerase II
C	0006914	biological_process	autophagy
C	0007031	biological_process	peroxisome organization
C	0016208	molecular_function	AMP binding
C	0019887	molecular_function	protein kinase regulator activity
C	0019901	molecular_function	protein kinase binding
C	0030447	biological_process	filamentous growth
C	0031588	cellular_component	nucleotide-activated protein kinase complex
C	0042149	biological_process	cellular response to glucose starvation
C	0042802	molecular_function	identical protein binding
C	0043539	molecular_function	protein serine/threonine kinase activator activity
C	0045722	biological_process	positive regulation of gluconeogenesis
C	1904547	biological_process	regulation of cellular response to glucose starvation
C	2000217	biological_process	regulation of invasive growth in response to glucose limitation
F	0000166	molecular_function	nucleotide binding
F	0004679	molecular_function	AMP-activated protein kinase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005641	cellular_component	nuclear envelope lumen
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006110	biological_process	regulation of glycolytic process
F	0006351	biological_process	DNA-templated transcription
F	0006357	biological_process	regulation of transcription by RNA polymerase II
F	0006914	biological_process	autophagy
F	0007031	biological_process	peroxisome organization
F	0016208	molecular_function	AMP binding
F	0019887	molecular_function	protein kinase regulator activity
F	0019901	molecular_function	protein kinase binding
F	0030447	biological_process	filamentous growth
F	0031588	cellular_component	nucleotide-activated protein kinase complex
F	0042149	biological_process	cellular response to glucose starvation
F	0042802	molecular_function	identical protein binding
F	0043539	molecular_function	protein serine/threonine kinase activator activity
F	0045722	biological_process	positive regulation of gluconeogenesis
F	1904547	biological_process	regulation of cellular response to glucose starvation
F	2000217	biological_process	regulation of invasive growth in response to glucose limitation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"24108357","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	120
Details	Domain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	118
Details	Domain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q10343","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22019086","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T4N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---