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6B2E

Structure of full length human AMPK (a2b2g1) in complex with a small molecule activator SC4.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003682molecular_functionchromatin binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006468biological_processprotein phosphorylation
A0006633biological_processfatty acid biosynthetic process
A0006695biological_processcholesterol biosynthetic process
A0006914biological_processautophagy
A0007165biological_processsignal transduction
A0008610biological_processlipid biosynthetic process
A0010468biological_processregulation of gene expression
A0010494cellular_componentcytoplasmic stress granule
A0010508biological_processpositive regulation of autophagy
A0010629biological_processnegative regulation of gene expression
A0014850biological_processresponse to muscle activity
A0016055biological_processWnt signaling pathway
A0016239biological_processpositive regulation of macroautophagy
A0016241biological_processregulation of macroautophagy
A0016607cellular_componentnuclear speck
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0031331biological_processpositive regulation of cellular catabolic process
A0031588cellular_componentnucleotide-activated protein kinase complex
A0031669biological_processcellular response to nutrient levels
A0032007biological_processnegative regulation of TOR signaling
A0034599biological_processcellular response to oxidative stress
A0042149biological_processcellular response to glucose starvation
A0042593biological_processglucose homeostasis
A0042752biological_processregulation of circadian rhythm
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0045821biological_processpositive regulation of glycolytic process
A0046872molecular_functionmetal ion binding
A0047322molecular_function[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity
A0048511biological_processrhythmic process
A0050405molecular_functionobsolete [acetyl-CoA carboxylase] kinase activity
A0055089biological_processfatty acid homeostasis
A0062028biological_processregulation of stress granule assembly
A0070507biological_processregulation of microtubule cytoskeleton organization
A0071277biological_processcellular response to calcium ion
A0071333biological_processcellular response to glucose stimulus
A0071380biological_processcellular response to prostaglandin E stimulus
A0071466biological_processcellular response to xenobiotic stimulus
A0097009biological_processenergy homeostasis
A0106310molecular_functionprotein serine kinase activity
A0140823molecular_functionhistone H2BS36 kinase activity
A1903829biological_processpositive regulation of protein localization
A1903944biological_processnegative regulation of hepatocyte apoptotic process
A1904262biological_processnegative regulation of TORC1 signaling
A1904428biological_processnegative regulation of tubulin deacetylation
A1905691biological_processlipid droplet disassembly
A1990044biological_processprotein localization to lipid droplet
A2000758biological_processpositive regulation of peptidyl-lysine acetylation
B0004679molecular_functionAMP-activated protein kinase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006633biological_processfatty acid biosynthetic process
B0007165biological_processsignal transduction
B0019901molecular_functionprotein kinase binding
B0031588cellular_componentnucleotide-activated protein kinase complex
B0031669biological_processcellular response to nutrient levels
B0120162biological_processpositive regulation of cold-induced thermogenesis
C0004672molecular_functionprotein kinase activity
C0004691molecular_functioncAMP-dependent protein kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006110biological_processregulation of glycolytic process
C0006468biological_processprotein phosphorylation
C0006633biological_processfatty acid biosynthetic process
C0007165biological_processsignal transduction
C0007283biological_processspermatogenesis
C0008603molecular_functioncAMP-dependent protein kinase regulator activity
C0010628biological_processpositive regulation of gene expression
C0016020cellular_componentmembrane
C0016208molecular_functionAMP binding
C0019887molecular_functionprotein kinase regulator activity
C0019901molecular_functionprotein kinase binding
C0031588cellular_componentnucleotide-activated protein kinase complex
C0031669biological_processcellular response to nutrient levels
C0043531molecular_functionADP binding
C0045860biological_processpositive regulation of protein kinase activity
C0051170biological_processimport into nucleus
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKiGehqltghk..........VAVK
ChainResidueDetails
ALEU22-LYS45

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL
ChainResidueDetails
AVAL135-LEU147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P80385
ChainResidueDetails
CVAL130
CARG152
CLYS170
CSER242
CARG269
CLEU277
CARG70
CMET85

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
ChainResidueDetails
CALA205
CSER226
CHIS298
CSER314
CHIS151
CTHR200

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385
ChainResidueDetails
CSER261
CSER270

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385
ChainResidueDetails
CTHR263
BSER158
BSER170

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSEP108

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTHR148

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER184

219869

PDB entries from 2024-05-15

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