AAKG1_HUMAN - dbPTM
AAKG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAKG1_HUMAN
UniProt AC P54619
Protein Name 5'-AMP-activated protein kinase subunit gamma-1
Gene Name PRKAG1
Organism Homo sapiens (Human).
Sequence Length 331
Subcellular Localization
Protein Description AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive..
Protein Sequence METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
6Phosphoserine--METVISSDSSPAV
--CCCCCCCHHCCCH
24.6125627689
7Phosphoserine-METVISSDSSPAVE
-CCCCCCCHHCCCHH
30.3225627689
9PhosphoserineETVISSDSSPAVENE
CCCCCCHHCCCHHHC
39.9225627689
10PhosphoserineTVISSDSSPAVENEH
CCCCCHHCCCHHHCC
23.1372265419
81PhosphoserineLWDSKKQSFVGMLTI
EEECCCCEEEEEEEC
30.6824667141
89PhosphothreonineFVGMLTITDFINILH
EEEEEECHHHHHHHH
21.4424667141
101PhosphoserineILHRYYKSALVQIYE
HHHHHHHHHHHHHHH
15.6618691976
107PhosphotyrosineKSALVQIYELEEHKI
HHHHHHHHHHHHHHH
9.4346163123
170UbiquitinlysineTLYILTHKRILKFLK
EEEEEECHHHHHHHH
35.5821906983
21890473
179UbiquitinlysineILKFLKLFITEFPKP
HHHHHHHHHHHHCCH
6.5821890473
179UbiquitinlysineILKFLKLFITEFPKP
HHHHHHHHHHHHCCH
6.5821906983
21890473
179UbiquitinlysineILKFLKLFITEFPKP
HHHHHHHHHHHHCCH
6.5821890473
232N6-acetyllysineVSALPVVDEKGRVVD
CCEEEEECCCCEEEE
52.7219608861
232UbiquitinlysineVSALPVVDEKGRVVD
CCEEEEECCCCEEEE
52.7219608861
234UbiquitinlysineALPVVDEKGRVVDIY
EEEEECCCCEEEEEE
47.7721906983
21890473
241PhosphotyrosineKGRVVDIYSKFDVIN
CCEEEEEEEHHHHHH
11.0123090842
242PhosphoserineGRVVDIYSKFDVINL
CEEEEEEEHHHHHHH
27.4723090842
243UbiquitinlysineRVVDIYSKFDVINLA
EEEEEEEHHHHHHHH
28.7221906983
21890473
253UbiquitinlysineVINLAAEKTYNNLDV
HHHHHHCCCCCCCCC
52.1321906983
21890473
261PhosphoserineTYNNLDVSVTKALQH
CCCCCCCCHHHHEEE
24.6019060867
263PhosphothreonineNNLDVSVTKALQHRS
CCCCCCHHHHEEECC
11.7719060867
264N6-acetyllysineNLDVSVTKALQHRSH
CCCCCHHHHEEECCC
44.9719608861
22424773
23236377
23954790
264N6-malonyllysineNLDVSVTKALQHRSH
CCCCCHHHHEEECCC
44.9726320211
270PhosphoserineTKALQHRSHYFEGVL
HHHEEECCCCCCCCE
22.0319060867
272PhosphotyrosineALQHRSHYFEGVLKC
HEEECCCCCCCCEEE
12.4620562877
273UbiquitinlysineLQHRSHYFEGVLKCY
EEECCCCCCCCEEEC
5.7321890473
273N6-acetyllysineLQHRSHYFEGVLKCY
EEECCCCCCCCEEEC
5.7319608861
273UbiquitinlysineLQHRSHYFEGVLKCY
EEECCCCCCCCEEEC
5.7319608861
273UbiquitinlysineLQHRSHYFEGVLKCY
EEECCCCCCCCEEEC
5.7321890473

Disease-associated PTM Sites based on nsSNP

* Distance = the distance between SNP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SNP Related Disease Reference
81Phosphorylation89 (8)TSrs1126930--
89Phosphorylation89 (0)TSrs1126930--

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AAKG2_HUMANPRKAG2physical
10698692
AAPK1_HUMANPRKAA1physical
10698692
AAPK2_HUMANPRKAA2physical
10698692
AAKB1_HUMANPRKAB1physical
10698692
AAKB2_HUMANPRKAB2physical
10698692
AAPK2_HUMANPRKAA2physical
20562859
AAPK1_HUMANPRKAA1physical
20562859
AAKB2_HUMANPRKAB2physical
20562859
AAKB1_HUMANPRKAB1physical
20562859
FKBP4_HUMANFKBP4physical
20562859
PGK1_HUMANPGK1physical
20562859
MCM2_HUMANMCM2physical
20562859
PA2G4_HUMANPA2G4physical
20562859
SYTC_HUMANTARSphysical
20562859
AAKG2_HUMANPRKAG2physical
20562859
ACACA_HUMANACACAphysical
18480843
AAKB1_HUMANPRKAB1physical
8621713
SNF1_YEASTSNF1physical
8621713
SIP1_YEASTSIP1physical
8621713
SIP2_YEASTSIP2physical
8621713
AAPK1_HUMANPRKAA1physical
8621713
AAKB1_HUMANPRKAB1physical
8663446
AAPK1_HUMANPRKAA1physical
8663446
KEAP1_HUMANKEAP1physical
25416956
TEKT1_HUMANTEKT1physical
25416956
CA094_HUMANC1orf94physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
TBB8_HUMANTUBB8physical
26186194
AT2B3_HUMANATP2B3physical
26186194
AAPK1_HUMANPRKAA1physical
26186194
AAPK2_HUMANPRKAA2physical
26186194
AAKB1_HUMANPRKAB1physical
26186194
AAKB2_HUMANPRKAB2physical
26186194
TNR6_HUMANFASphysical
26186194
GLMP_HUMANC1orf85physical
26186194
MFS4B_HUMANKIAA1919physical
26186194
INT14_HUMANVWA9physical
26186194
GTR8_HUMANSLC2A8physical
26186194
EIF3G_HUMANEIF3Gphysical
21516116
AAKB2_HUMANPRKAB2physical
28514442
AAKB1_HUMANPRKAB1physical
28514442
AAPK2_HUMANPRKAA2physical
28514442
AAPK1_HUMANPRKAA1physical
28514442
AT2B3_HUMANATP2B3physical
28514442
MFS4B_HUMANKIAA1919physical
28514442
GLMP_HUMANC1orf85physical
28514442
GTR8_HUMANSLC2A8physical
28514442
TBB8_HUMANTUBB8physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00945Acetylsalicylic acid
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, AND MASS SPECTROMETRY.

TOP