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
1Acetylation-------METVISSD
-------CCEECCCC		9.82-
6Phosphorylation--METVISSDSSPAV
--CCEECCCCCCCCC		24.6125159151
7Phosphorylation-METVISSDSSPAVE
-CCEECCCCCCCCCC		30.3225159151
9PhosphorylationETVISSDSSPAVENE
CEECCCCCCCCCCCC		39.9222199227
10PhosphorylationTVISSDSSPAVENEH
EECCCCCCCCCCCCC		23.1322199227
21PhosphorylationENEHPQETPESNNSV
CCCCCCCCCCCCCHH		27.4026074081
24PhosphorylationHPQETPESNNSVYTS
CCCCCCCCCCHHHHH		42.3826074081
27PhosphorylationETPESNNSVYTSFMK
CCCCCCCHHHHHHHH		22.2826074081
34UbiquitinationSVYTSFMKSHRCYDL
HHHHHHHHHCCCCHH		40.89-
34MethylationSVYTSFMKSHRCYDL
HHHHHHHHHCCCCHH		40.89-
39PhosphorylationFMKSHRCYDLIPTSS
HHHHCCCCHHCCCCC		17.4622210691
45PhosphorylationCYDLIPTSSKLVVFD
CCHHCCCCCCEEEEE		21.8122210691
46PhosphorylationYDLIPTSSKLVVFDT
CHHCCCCCCEEEEEC		32.2722210691
78UbiquitinationAAPLWDSKKQSFVGM
EECCCCCCCCCCCCC		52.97-
81PhosphorylationLWDSKKQSFVGMLTI
CCCCCCCCCCCCCHH		30.6824667141
89PhosphorylationFVGMLTITDFINILH
CCCCCHHHHHHHHHH		21.4424667141
101PhosphorylationILHRYYKSALVQIYE
HHHHHHHHHHHHHHC		15.6618691976
107PhosphorylationKSALVQIYELEEHKI
HHHHHHHHCHHHHCC		9.4346163123
116PhosphorylationLEEHKIETWREVYLQ
HHHHCCCHHHHHHCC		33.0427642862
144PhosphorylationSLFDAVSSLIRNKIH
HHHHHHHHHHHHCCC		22.6324719451
170UbiquitinationTLYILTHKRILKFLK
EEEEEEHHHHHHHHH		35.5821890473
174UbiquitinationLTHKRILKFLKLFIT
EEHHHHHHHHHHHHH		46.40-
179UbiquitinationILKFLKLFITEFPKP
HHHHHHHHHHCCCCH		6.5821890473
179UbiquitinationILKFLKLFITEFPKP
HHHHHHHHHHCCCCH		6.5821890473
179UbiquitinationILKFLKLFITEFPKP
HHHHHHHHHHCCCCH		6.5821890473
192PhosphorylationKPEFMSKSLEELQIG
CHHHHCCCHHHHCCC		33.4324043423
200PhosphorylationLEELQIGTYANIAMV
HHHHCCCCCCCEEEE		22.5324043423
201PhosphorylationEELQIGTYANIAMVR
HHHCCCCCCCEEEEE		7.7624043423
232AcetylationVSALPVVDEKGRVVD
CCCCCEECCCCCEEE		52.7219608861
232UbiquitinationVSALPVVDEKGRVVD
CCCCCEECCCCCEEE		52.7219608861
234UbiquitinationALPVVDEKGRVVDIY
CCCEECCCCCEEEEE		47.7721890473
241PhosphorylationKGRVVDIYSKFDVIN
CCCEEEEECCCCCCH		11.0123090842
242PhosphorylationGRVVDIYSKFDVINL
CCEEEEECCCCCCHH		27.4723090842
243UbiquitinationRVVDIYSKFDVINLA
CEEEEECCCCCCHHH		28.7221890473
253UbiquitinationVINLAAEKTYNNLDV
CCHHHHHHHCCCCCH		52.1321890473
254PhosphorylationINLAAEKTYNNLDVS
CHHHHHHHCCCCCHH		24.0030622161
255PhosphorylationNLAAEKTYNNLDVSV
HHHHHHHCCCCCHHH		17.0829496907
261PhosphorylationTYNNLDVSVTKALQH
HCCCCCHHHHHHHHC		24.6021082442
263PhosphorylationNNLDVSVTKALQHRS
CCCCHHHHHHHHCCC		11.7721082442
264AcetylationNLDVSVTKALQHRSH
CCCHHHHHHHHCCCH		44.9723954790
264MalonylationNLDVSVTKALQHRSH
CCCHHHHHHHHCCCH		44.9726320211
264UbiquitinationNLDVSVTKALQHRSH
CCCHHHHHHHHCCCH		44.9721890473
270PhosphorylationTKALQHRSHYFEGVL
HHHHHCCCHHHHHHH		22.0321082442
272PhosphorylationALQHRSHYFEGVLKC
HHHCCCHHHHHHHHH		12.4628796482
273UbiquitinationLQHRSHYFEGVLKCY
HHCCCHHHHHHHHHH		5.7319608861
273UbiquitinationLQHRSHYFEGVLKCY
HHCCCHHHHHHHHHH		5.7321890473
273AcetylationLQHRSHYFEGVLKCY
HHCCCHHHHHHHHHH		5.7319608861
273UbiquitinationLQHRSHYFEGVLKCY
HHCCCHHHHHHHHHH		5.7321890473
281PhosphorylationEGVLKCYLHETLETI
HHHHHHHHHHHHHHH		4.0527642862
284PhosphorylationLKCYLHETLETIINR
HHHHHHHHHHHHHHH		21.10-
314PhosphorylationDVVKGIVSLSDILQA
HHHCCCCCHHHHHHH		21.8930622161
316PhosphorylationVKGIVSLSDILQALV
HCCCCCHHHHHHHHH		18.3330622161
325PhosphorylationILQALVLTGGEKKP-
HHHHHHHCCCCCCC-		35.3430622161
329UbiquitinationLVLTGGEKKP-----
HHHCCCCCCC-----		73.88-
330UbiquitinationVLTGGEKKP------
HHCCCCCCC------		52.21-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
192SPhosphorylationKinaseDNAPKP78527
PSP
261SPhosphorylationKinaseULK1O75385
Uniprot
263TPhosphorylationKinaseULK1O75385
Uniprot
270SPhosphorylationKinaseULK1O75385
Uniprot
284TPhosphorylationKinaseDNAPKP78527
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAKG1_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AAKG1_HUMAN !!
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
Regulatory Network of AAKG1_HUMAN

loading...

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
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory