AAKG2_MOUSE - dbPTM
AAKG2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAKG2_MOUSE
UniProt AC Q91WG5
Protein Name 5'-AMP-activated protein kinase subunit gamma-2
Gene Name Prkag2
Organism Mus musculus (Mouse).
Sequence Length 566
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 (By similarity)..
Protein Sequence MGSAAMDTKKKKEVSSPGGSSGKKNPSLKRRSLRVHIPDLSSFAMPLLDGDVENSEKHSSRKVDSPFSSGSPSRGLFSRGPQPRPSSPVSAPVRPKTSPGSPKTVFPFSYQESPPRSPRRMSFSGIFRSSSKESSPNSNPSTSPGGIRFFSRSRKTSSVSSSPSTPTQVTKQHPFPLESYKQEPERPESRIYASSSPPDTGQRFCLAFQSPARPPLASPTYHAPLRTAVLAAAPGPAEAGMLEKLEFQEEEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCSKLETLETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
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
15PhosphorylationTKKKKEVSSPGGSSG
CCCCCCCCCCCCCCC
31.7229899451
16PhosphorylationKKKKEVSSPGGSSGK
CCCCCCCCCCCCCCC
32.5127841257
21PhosphorylationVSSPGGSSGKKNPSL
CCCCCCCCCCCCHHH
58.8829899451
32PhosphorylationNPSLKRRSLRVHIPD
CHHHHCCEEEEECCC
25.2620811261
41PhosphorylationRVHIPDLSSFAMPLL
EEECCCHHHHCHHCC
30.6923984901
42PhosphorylationVHIPDLSSFAMPLLD
EECCCHHHHCHHCCC
25.0723984901
65PhosphorylationHSSRKVDSPFSSGSP
HCCCCCCCCCCCCCC
30.7225521595
68PhosphorylationRKVDSPFSSGSPSRG
CCCCCCCCCCCCCCC
36.8523684622
69PhosphorylationKVDSPFSSGSPSRGL
CCCCCCCCCCCCCCC
43.6023684622
71PhosphorylationDSPFSSGSPSRGLFS
CCCCCCCCCCCCCCC
22.9625521595
73PhosphorylationPFSSGSPSRGLFSRG
CCCCCCCCCCCCCCC
40.4521082442
78PhosphorylationSPSRGLFSRGPQPRP
CCCCCCCCCCCCCCC
41.1722817900
86PhosphorylationRGPQPRPSSPVSAPV
CCCCCCCCCCCCCCC
48.8623684622
87PhosphorylationGPQPRPSSPVSAPVR
CCCCCCCCCCCCCCC
31.8125521595
90PhosphorylationPRPSSPVSAPVRPKT
CCCCCCCCCCCCCCC
30.1825521595
97PhosphorylationSAPVRPKTSPGSPKT
CCCCCCCCCCCCCCE
42.7221183079
101PhosphorylationRPKTSPGSPKTVFPF
CCCCCCCCCCEECCC
26.977602467
104PhosphorylationTSPGSPKTVFPFSYQ
CCCCCCCEECCCCCC
30.6623984901
109PhosphorylationPKTVFPFSYQESPPR
CCEECCCCCCCCCCC
26.5881018321
110PhosphorylationKTVFPFSYQESPPRS
CEECCCCCCCCCCCC
19.3726643407
113PhosphorylationFPFSYQESPPRSPRR
CCCCCCCCCCCCCCC
25.3625521595
117PhosphorylationYQESPPRSPRRMSFS
CCCCCCCCCCCCCEE
28.6525521595
122PhosphorylationPRSPRRMSFSGIFRS
CCCCCCCCEEEECCC
17.9123684622
124PhosphorylationSPRRMSFSGIFRSSS
CCCCCCEEEECCCCC
24.5421743459
129PhosphorylationSFSGIFRSSSKESSP
CEEEECCCCCCCCCC
28.3724759943
130PhosphorylationFSGIFRSSSKESSPN
EEEECCCCCCCCCCC
40.9722817900
131PhosphorylationSGIFRSSSKESSPNS
EEECCCCCCCCCCCC
41.5129899451
134PhosphorylationFRSSSKESSPNSNPS
CCCCCCCCCCCCCCC
55.6323684622
135PhosphorylationRSSSKESSPNSNPST
CCCCCCCCCCCCCCC
29.2325521595
138PhosphorylationSKESSPNSNPSTSPG
CCCCCCCCCCCCCCC
54.2023684622
141PhosphorylationSSPNSNPSTSPGGIR
CCCCCCCCCCCCCEE
45.8522324799
142PhosphorylationSPNSNPSTSPGGIRF
CCCCCCCCCCCCEEE
39.9523684622
143PhosphorylationPNSNPSTSPGGIRFF
CCCCCCCCCCCEEEE
26.3625521595
151PhosphorylationPGGIRFFSRSRKTSS
CCCEEEEECCCCCCC
27.0023984901
156PhosphorylationFFSRSRKTSSVSSSP
EEECCCCCCCCCCCC
25.7329472430
157PhosphorylationFSRSRKTSSVSSSPS
EECCCCCCCCCCCCC
31.6025521595
158PhosphorylationSRSRKTSSVSSSPST
ECCCCCCCCCCCCCC
31.1129899451
160PhosphorylationSRKTSSVSSSPSTPT
CCCCCCCCCCCCCCC
27.3529899451
161PhosphorylationRKTSSVSSSPSTPTQ
CCCCCCCCCCCCCCC
44.0825521595
162PhosphorylationKTSSVSSSPSTPTQV
CCCCCCCCCCCCCCC
18.5025521595
164PhosphorylationSSVSSSPSTPTQVTK
CCCCCCCCCCCCCCC
49.3025521595
165PhosphorylationSVSSSPSTPTQVTKQ
CCCCCCCCCCCCCCC
33.4725521595
167PhosphorylationSSSPSTPTQVTKQHP
CCCCCCCCCCCCCCC
35.4419060867
170PhosphorylationPSTPTQVTKQHPFPL
CCCCCCCCCCCCCCH
18.3729472430
180PhosphorylationHPFPLESYKQEPERP
CCCCHHHHCCCCCCC
13.8122871156
192PhosphorylationERPESRIYASSSPPD
CCCCCCEEECCCCCC
10.1830635358
194PhosphorylationPESRIYASSSPPDTG
CCCCEEECCCCCCCC
17.8730635358
195PhosphorylationESRIYASSSPPDTGQ
CCCEEECCCCCCCCC
38.4025521595
196PhosphorylationSRIYASSSPPDTGQR
CCEEECCCCCCCCCC
37.6525521595
200PhosphorylationASSSPPDTGQRFCLA
ECCCCCCCCCCEEEE
40.7727742792
210PhosphorylationRFCLAFQSPARPPLA
CEEEEECCCCCCCCC
17.6724759943
218PhosphorylationPARPPLASPTYHAPL
CCCCCCCCCCCCCCH
26.009536077
220PhosphorylationRPPLASPTYHAPLRT
CCCCCCCCCCCCHHH
25.9923984901
221PhosphorylationPPLASPTYHAPLRTA
CCCCCCCCCCCHHHH
10.2023984901

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAKG2_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AAKG2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AAKG2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-71; SER-73;SER-90; SER-138; SER-158; SER-161 AND SER-162, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND MASSSPECTROMETRY.

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