AAKG2_HUMAN - dbPTM
AAKG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAKG2_HUMAN
UniProt AC Q9UGJ0
Protein Name 5'-AMP-activated protein kinase subunit gamma-2
Gene Name PRKAG2
Organism Homo sapiens (Human).
Sequence Length 569
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 MGSAVMDTKKKKDVSSPGGSGGKKNASQKRRSLRVHIPDLSSFAMPLLDGDLEGSGKHSSRKVDSPFGPGSPSKGFFSRGPQPRPSSPMSAPVRPKTSPGSPKTVFPFSYQESPPRSPRRMSFSGIFRSSSKESSPNSNPATSPGGIRFFSRSRKTSGLSSSPSTPTQVTKQHTFPLESYKHEPERLENRIYASSSPPDTGQRFCPSSFQSPTRPPLASPTHYAPSKAAALAAALGPAEAGMLEKLEFEDEAVEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
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
9AcetylationGSAVMDTKKKKDVSS
CCCCCCCCCCCCCCC		59.3319608861
15PhosphorylationTKKKKDVSSPGGSGG
CCCCCCCCCCCCCCC		40.7328985074
16O-linked_GlycosylationKKKKDVSSPGGSGGK
CCCCCCCCCCCCCCC		27.6730379171
27PhosphorylationSGGKKNASQKRRSLR
CCCCCCHHHHHHHHE		45.7018691976
32PhosphorylationNASQKRRSLRVHIPD
CHHHHHHHHEEECCC		25.2620860994
41PhosphorylationRVHIPDLSSFAMPLL
EEECCCHHHHCCCCC		30.6920860994
42PhosphorylationVHIPDLSSFAMPLLD
EECCCHHHHCCCCCC		25.0720860994
55PhosphorylationLDGDLEGSGKHSSRK
CCCCCCCCCCCCCCC		34.9820860994
59PhosphorylationLEGSGKHSSRKVDSP
CCCCCCCCCCCCCCC		35.0122210691
60PhosphorylationEGSGKHSSRKVDSPF
CCCCCCCCCCCCCCC		35.5222210691
62MethylationSGKHSSRKVDSPFGP
CCCCCCCCCCCCCCC		52.95-
65PhosphorylationHSSRKVDSPFGPGSP
CCCCCCCCCCCCCCC		25.7223927012
71PhosphorylationDSPFGPGSPSKGFFS
CCCCCCCCCCCCCCC		29.1823401153
73PhosphorylationPFGPGSPSKGFFSRG
CCCCCCCCCCCCCCC		47.2923927012
78PhosphorylationSPSKGFFSRGPQPRP
CCCCCCCCCCCCCCC		33.7828152594
86PhosphorylationRGPQPRPSSPMSAPV
CCCCCCCCCCCCCCC		48.6430576142
87PhosphorylationGPQPRPSSPMSAPVR
CCCCCCCCCCCCCCC		27.5725849741
90PhosphorylationPRPSSPMSAPVRPKT
CCCCCCCCCCCCCCC		32.5730576142
97PhosphorylationSAPVRPKTSPGSPKT
CCCCCCCCCCCCCCE		42.7230576142
98PhosphorylationAPVRPKTSPGSPKTV
CCCCCCCCCCCCCEE		33.1326657352
101PhosphorylationRPKTSPGSPKTVFPF
CCCCCCCCCCEECCC		26.977602463
104PhosphorylationTSPGSPKTVFPFSYQ
CCCCCCCEECCCCCC		30.6627080861
109PhosphorylationPKTVFPFSYQESPPR
CCEECCCCCCCCCCC		26.5828857561
110PhosphorylationKTVFPFSYQESPPRS
CEECCCCCCCCCCCC		19.3727080861
113PhosphorylationFPFSYQESPPRSPRR
CCCCCCCCCCCCCCC		25.3617525332
117PhosphorylationYQESPPRSPRRMSFS
CCCCCCCCCCCCCEE		28.6528258704
122PhosphorylationPRSPRRMSFSGIFRS
CCCCCCCCEEECCCC		17.919535961
124PhosphorylationSPRRMSFSGIFRSSS
CCCCCCEEECCCCCC		24.5428857561
129PhosphorylationSFSGIFRSSSKESSP
CEEECCCCCCCCCCC		28.3720068231
130PhosphorylationFSGIFRSSSKESSPN
EEECCCCCCCCCCCC		40.97104451
131PhosphorylationSGIFRSSSKESSPNS
EECCCCCCCCCCCCC		41.5126657352
134PhosphorylationFRSSSKESSPNSNPA
CCCCCCCCCCCCCCC		55.6322777824
135PhosphorylationRSSSKESSPNSNPAT
CCCCCCCCCCCCCCC		29.239536011
138PhosphorylationSKESSPNSNPATSPG
CCCCCCCCCCCCCCC		47.8020068231
142PhosphorylationSPNSNPATSPGGIRF
CCCCCCCCCCCCEEE		36.3919369195
143PhosphorylationPNSNPATSPGGIRFF
CCCCCCCCCCCEEEE		24.5323401153
151PhosphorylationPGGIRFFSRSRKTSG
CCCEEEEECCCCCCC		27.0020068231
153PhosphorylationGIRFFSRSRKTSGLS
CEEEEECCCCCCCCC		36.6114646071
156PhosphorylationFFSRSRKTSGLSSSP
EEECCCCCCCCCCCC		27.2426657352
157PhosphorylationFSRSRKTSGLSSSPS
EECCCCCCCCCCCCC		40.5517525332
160PhosphorylationSRKTSGLSSSPSTPT
CCCCCCCCCCCCCCC		32.0928450419
161PhosphorylationRKTSGLSSSPSTPTQ
CCCCCCCCCCCCCCC		51.8426657352
162PhosphorylationKTSGLSSSPSTPTQV
CCCCCCCCCCCCCCC		21.3517525332
164PhosphorylationSGLSSSPSTPTQVTK
CCCCCCCCCCCCCCC		49.3028450419
165PhosphorylationGLSSSPSTPTQVTKQ
CCCCCCCCCCCCCCC		33.4726657352
167PhosphorylationSSSPSTPTQVTKQHT
CCCCCCCCCCCCCCC		35.4417525332
170PhosphorylationPSTPTQVTKQHTFPL
CCCCCCCCCCCCCCC		18.3728450419
180PhosphorylationHTFPLESYKHEPERL
CCCCCHHHCCCHHHH		13.6422817900
192PhosphorylationERLENRIYASSSPPD
HHHHCCEECCCCCCC		9.3725348954
194PhosphorylationLENRIYASSSPPDTG
HHCCEECCCCCCCCC		17.8728450419
195PhosphorylationENRIYASSSPPDTGQ
HCCEECCCCCCCCCC		38.4028102081
196PhosphorylationNRIYASSSPPDTGQR
CCEECCCCCCCCCCC		37.6525159151
200PhosphorylationASSSPPDTGQRFCPS
CCCCCCCCCCCCCCC		40.7728450419
207PhosphorylationTGQRFCPSSFQSPTR
CCCCCCCCCCCCCCC		44.9928857561
208PhosphorylationGQRFCPSSFQSPTRP
CCCCCCCCCCCCCCC		16.6728857561
211PhosphorylationFCPSSFQSPTRPPLA
CCCCCCCCCCCCCCC		26.6528152594
213PhosphorylationPSSFQSPTRPPLASP
CCCCCCCCCCCCCCC		62.1428152594
219PhosphorylationPTRPPLASPTHYAPS
CCCCCCCCCCCCCHH		37.7125159151
221PhosphorylationRPPLASPTHYAPSKA
CCCCCCCCCCCHHHH		25.6428152594
223PhosphorylationPLASPTHYAPSKAAA
CCCCCCCCCHHHHHH		23.7628857561
226PhosphorylationSPTHYAPSKAAALAA
CCCCCCHHHHHHHHH		27.1028152594
309PhosphorylationRAAPLWESKKQSFVG
EECCHHHCCCCCCCC		33.3020071362
313PhosphorylationLWESKKQSFVGMLTI
HHHCCCCCCCCEEEH		30.6824667141
321PhosphorylationFVGMLTITDFINILH
CCCEEEHHHHHHHHH		21.4424667141
350 (in isoform 2)Ubiquitination-31.3121906983
376PhosphorylationSLFDAVYSLIKNKIH
HHHHHHHHHHHHCCC		19.6124719451
431 (in isoform 3)Ubiquitination-20.5821906983
466PhosphorylationALPVVDESGKVVDIY
CCCEECCCCCEEEEE		39.1820068231
475UbiquitinationKVVDIYSKFDVINLA
CEEEEEECCCHHHHH		28.72-
475 (in isoform 1)Ubiquitination-28.7221906983
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

Oops, there are no upstream regulatory protein records of AAKG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAKG2_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 AAKG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AAKB1_HUMANPRKAB1physical
10698692
AAKB2_HUMANPRKAB2physical
10698692
AAPK2_HUMANPRKAA2physical
20562859
AAKB2_HUMANPRKAB2physical
20562859
AAPK1_HUMANPRKAA1physical
20562859
AAKG1_HUMANPRKAG1physical
20562859
MAP1B_HUMANMAP1Bphysical
20562859
AAKB1_HUMANPRKAB1physical
20562859
MLP3A_HUMANMAP1LC3Aphysical
20562859
PGK1_HUMANPGK1physical
20562859
PUR4_HUMANPFASphysical
20562859
FKBP4_HUMANFKBP4physical
20562859
EIF3A_HUMANEIF3Aphysical
20562859
SYTC_HUMANTARSphysical
20562859
GUAA_HUMANGMPSphysical
20562859
GANAB_HUMANGANABphysical
20562859
MAP1A_HUMANMAP1Aphysical
20562859
ASNS_HUMANASNSphysical
20562859
AAPK1_HUMANPRKAA1physical
26186194
AAPK2_HUMANPRKAA2physical
26186194
AAKB1_HUMANPRKAB1physical
26186194
AAKB2_HUMANPRKAB2physical
26186194
AAKB2_HUMANPRKAB2physical
28514442
AAKB1_HUMANPRKAB1physical
28514442
AAPK2_HUMANPRKAA2physical
28514442
AAPK1_HUMANPRKAA1physical
28514442
GEMI2_HUMANGEMIN2physical
28514442
NFH_HUMANNEFHphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
194200Wolff-Parkinson-White syndrome (WPWS)
600858Cardiomyopathy, familial hypertrophic 6 (CMH6)
261740Glycogen storage disease of heart lethal congenital (GSDH)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00945Acetylsalicylic acid
Regulatory Network of AAKG2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-71; SER-86;SER-131; SER-134; SER-135; SER-138; THR-142; SER-143; THR-156;SER-157; SER-160; SER-162; SER-164; SER-195; SER-196 AND SER-219, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-130; SER-143;SER-162; SER-164; THR-165 AND SER-196, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-143 AND SER-196,AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-162 ANDTHR-167, AND MASS SPECTROMETRY.

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