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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
15 | Phosphorylation | TKKKKEVSSPGGSSG CCCCCCCCCCCCCCC | 31.72 | 29899451 | |
16 | Phosphorylation | KKKKEVSSPGGSSGK CCCCCCCCCCCCCCC | 32.51 | 27841257 | |
21 | Phosphorylation | VSSPGGSSGKKNPSL CCCCCCCCCCCCHHH | 58.88 | 29899451 | |
32 | Phosphorylation | NPSLKRRSLRVHIPD CHHHHCCEEEEECCC | 25.26 | 20811261 | |
41 | Phosphorylation | RVHIPDLSSFAMPLL EEECCCHHHHCHHCC | 30.69 | 23984901 | |
42 | Phosphorylation | VHIPDLSSFAMPLLD EECCCHHHHCHHCCC | 25.07 | 23984901 | |
65 | Phosphorylation | HSSRKVDSPFSSGSP HCCCCCCCCCCCCCC | 30.72 | 25521595 | |
68 | Phosphorylation | RKVDSPFSSGSPSRG CCCCCCCCCCCCCCC | 36.85 | 23684622 | |
69 | Phosphorylation | KVDSPFSSGSPSRGL CCCCCCCCCCCCCCC | 43.60 | 23684622 | |
71 | Phosphorylation | DSPFSSGSPSRGLFS CCCCCCCCCCCCCCC | 22.96 | 25521595 | |
73 | Phosphorylation | PFSSGSPSRGLFSRG CCCCCCCCCCCCCCC | 40.45 | 21082442 | |
78 | Phosphorylation | SPSRGLFSRGPQPRP CCCCCCCCCCCCCCC | 41.17 | 22817900 | |
86 | Phosphorylation | RGPQPRPSSPVSAPV CCCCCCCCCCCCCCC | 48.86 | 23684622 | |
87 | Phosphorylation | GPQPRPSSPVSAPVR CCCCCCCCCCCCCCC | 31.81 | 25521595 | |
90 | Phosphorylation | PRPSSPVSAPVRPKT CCCCCCCCCCCCCCC | 30.18 | 25521595 | |
97 | Phosphorylation | SAPVRPKTSPGSPKT CCCCCCCCCCCCCCE | 42.72 | 21183079 | |
101 | Phosphorylation | RPKTSPGSPKTVFPF CCCCCCCCCCEECCC | 26.97 | 7602467 | |
104 | Phosphorylation | TSPGSPKTVFPFSYQ CCCCCCCEECCCCCC | 30.66 | 23984901 | |
109 | Phosphorylation | PKTVFPFSYQESPPR CCEECCCCCCCCCCC | 26.58 | 81018321 | |
110 | Phosphorylation | KTVFPFSYQESPPRS CEECCCCCCCCCCCC | 19.37 | 26643407 | |
113 | Phosphorylation | FPFSYQESPPRSPRR CCCCCCCCCCCCCCC | 25.36 | 25521595 | |
117 | Phosphorylation | YQESPPRSPRRMSFS CCCCCCCCCCCCCEE | 28.65 | 25521595 | |
122 | Phosphorylation | PRSPRRMSFSGIFRS CCCCCCCCEEEECCC | 17.91 | 23684622 | |
124 | Phosphorylation | SPRRMSFSGIFRSSS CCCCCCEEEECCCCC | 24.54 | 21743459 | |
129 | Phosphorylation | SFSGIFRSSSKESSP CEEEECCCCCCCCCC | 28.37 | 24759943 | |
130 | Phosphorylation | FSGIFRSSSKESSPN EEEECCCCCCCCCCC | 40.97 | 22817900 | |
131 | Phosphorylation | SGIFRSSSKESSPNS EEECCCCCCCCCCCC | 41.51 | 29899451 | |
134 | Phosphorylation | FRSSSKESSPNSNPS CCCCCCCCCCCCCCC | 55.63 | 23684622 | |
135 | Phosphorylation | RSSSKESSPNSNPST CCCCCCCCCCCCCCC | 29.23 | 25521595 | |
138 | Phosphorylation | SKESSPNSNPSTSPG CCCCCCCCCCCCCCC | 54.20 | 23684622 | |
141 | Phosphorylation | SSPNSNPSTSPGGIR CCCCCCCCCCCCCEE | 45.85 | 22324799 | |
142 | Phosphorylation | SPNSNPSTSPGGIRF CCCCCCCCCCCCEEE | 39.95 | 23684622 | |
143 | Phosphorylation | PNSNPSTSPGGIRFF CCCCCCCCCCCEEEE | 26.36 | 25521595 | |
151 | Phosphorylation | PGGIRFFSRSRKTSS CCCEEEEECCCCCCC | 27.00 | 23984901 | |
156 | Phosphorylation | FFSRSRKTSSVSSSP EEECCCCCCCCCCCC | 25.73 | 29472430 | |
157 | Phosphorylation | FSRSRKTSSVSSSPS EECCCCCCCCCCCCC | 31.60 | 25521595 | |
158 | Phosphorylation | SRSRKTSSVSSSPST ECCCCCCCCCCCCCC | 31.11 | 29899451 | |
160 | Phosphorylation | SRKTSSVSSSPSTPT CCCCCCCCCCCCCCC | 27.35 | 29899451 | |
161 | Phosphorylation | RKTSSVSSSPSTPTQ CCCCCCCCCCCCCCC | 44.08 | 25521595 | |
162 | Phosphorylation | KTSSVSSSPSTPTQV CCCCCCCCCCCCCCC | 18.50 | 25521595 | |
164 | Phosphorylation | SSVSSSPSTPTQVTK CCCCCCCCCCCCCCC | 49.30 | 25521595 | |
165 | Phosphorylation | SVSSSPSTPTQVTKQ CCCCCCCCCCCCCCC | 33.47 | 25521595 | |
167 | Phosphorylation | SSSPSTPTQVTKQHP CCCCCCCCCCCCCCC | 35.44 | 19060867 | |
170 | Phosphorylation | PSTPTQVTKQHPFPL CCCCCCCCCCCCCCH | 18.37 | 29472430 | |
180 | Phosphorylation | HPFPLESYKQEPERP CCCCHHHHCCCCCCC | 13.81 | 22871156 | |
192 | Phosphorylation | ERPESRIYASSSPPD CCCCCCEEECCCCCC | 10.18 | 30635358 | |
194 | Phosphorylation | PESRIYASSSPPDTG CCCCEEECCCCCCCC | 17.87 | 30635358 | |
195 | Phosphorylation | ESRIYASSSPPDTGQ CCCEEECCCCCCCCC | 38.40 | 25521595 | |
196 | Phosphorylation | SRIYASSSPPDTGQR CCEEECCCCCCCCCC | 37.65 | 25521595 | |
200 | Phosphorylation | ASSSPPDTGQRFCLA ECCCCCCCCCCEEEE | 40.77 | 27742792 | |
210 | Phosphorylation | RFCLAFQSPARPPLA CEEEEECCCCCCCCC | 17.67 | 24759943 | |
218 | Phosphorylation | PARPPLASPTYHAPL CCCCCCCCCCCCCCH | 26.00 | 9536077 | |
220 | Phosphorylation | RPPLASPTYHAPLRT CCCCCCCCCCCCHHH | 25.99 | 23984901 | |
221 | Phosphorylation | PPLASPTYHAPLRTA CCCCCCCCCCCHHHH | 10.20 | 23984901 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AAKG2_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of AAKG2_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"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. |