| UniProt ID | AAKB2_HUMAN | |
|---|---|---|
| UniProt AC | O43741 | |
| Protein Name | 5'-AMP-activated protein kinase subunit beta-2 | |
| Gene Name | PRKAB2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 272 | |
| Subcellular Localization | ||
| Protein Description | Non-catalytic 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. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).. | |
| Protein Sequence | MGNTTSDRVSGERHGAKAARSEGAGGHAPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVSWQQDLEDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYAFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSIKDSVMVLSATHRYKKKYVTTLLYKPI | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MGNTTSDRVSG ----CCCCHHHCCCC | 23.19 | 30576142 | |
| 6 | Phosphorylation | --MGNTTSDRVSGER --CCCCHHHCCCCCC | 22.75 | 30576142 | |
| 10 | Phosphorylation | NTTSDRVSGERHGAK CCHHHCCCCCCCCHH | 35.51 | 30576142 | |
| 21 | Phosphorylation | HGAKAARSEGAGGHA CCHHHHHCCCCCCCC | 35.34 | 22798277 | |
| 39 | Phosphorylation | EHKIMVGSTDDPSVF CCEEEEECCCCCCCC | 19.77 | 22167270 | |
| 40 | Phosphorylation | HKIMVGSTDDPSVFS CEEEEECCCCCCCCC | 38.19 | 22167270 | |
| 44 | Phosphorylation | VGSTDDPSVFSLPDS EECCCCCCCCCCCCC | 42.67 | 23663014 | |
| 47 | Phosphorylation | TDDPSVFSLPDSKLP CCCCCCCCCCCCCCC | 36.52 | 23403867 | |
| 51 | Phosphorylation | SVFSLPDSKLPGDKE CCCCCCCCCCCCCHH | 33.87 | 23403867 | |
| 57 | Ubiquitination | DSKLPGDKEFVSWQQ CCCCCCCHHHCCHHH | 59.99 | 29967540 | |
| 61 | Phosphorylation | PGDKEFVSWQQDLED CCCHHHCCHHHHHHH | 25.20 | 69008957 | |
| 69 | Phosphorylation | WQQDLEDSVKPTQQA HHHHHHHCCCCCCCC | 23.75 | 51555815 | |
| 71 | Ubiquitination | QDLEDSVKPTQQARP HHHHHCCCCCCCCCC | 46.42 | 29967540 | |
| 93 | Phosphorylation | GGKEVFISGSFNNWS CCCEEEEEECCCCCC | 19.54 | 50565011 | |
| 95 | Phosphorylation | KEVFISGSFNNWSTK CEEEEEECCCCCCCC | 20.29 | 28857561 | |
| 100 | Phosphorylation | SGSFNNWSTKIPLIK EECCCCCCCCCEEEE | 23.19 | 113301177 | |
| 108 | Phosphorylation | TKIPLIKSHNDFVAI CCCEEEECCCCEEEE | 22.11 | 25159151 | |
| 125 | Phosphorylation | LPEGEHQYKFFVDGQ CCCCCCEEEEEECCE | 16.21 | 25022875 | |
| 148 | Phosphorylation | VVTSQLGTINNLIHV EEEEECCCCCCEEEE | 29.17 | 20166139 | |
| 157 | Ubiquitination | NNLIHVKKSDFEVFD CCEEEECHHHCCCEE | 54.92 | 29967540 | |
| 158 | Phosphorylation | NLIHVKKSDFEVFDA CEEEECHHHCCCEEE | 41.64 | 25072903 | |
| 170 | Phosphorylation | FDALKLDSMESSETS EEEEECCCCCCCCCC | 34.58 | 23090842 | |
| 173 | Phosphorylation | LKLDSMESSETSCRD EECCCCCCCCCCHHH | 25.49 | 20166139 | |
| 174 | Phosphorylation | KLDSMESSETSCRDL ECCCCCCCCCCHHHC | 31.42 | 23090842 | |
| 176 | Phosphorylation | DSMESSETSCRDLSS CCCCCCCCCHHHCCC | 34.77 | 23090842 | |
| 177 | Phosphorylation | SMESSETSCRDLSSS CCCCCCCCHHHCCCC | 11.78 | 22210691 | |
| 182 | Phosphorylation | ETSCRDLSSSPPGPY CCCHHHCCCCCCCCC | 32.81 | 22167270 | |
| 183 | Phosphorylation | TSCRDLSSSPPGPYG CCHHHCCCCCCCCCC | 54.91 | 22167270 | |
| 184 | Phosphorylation | SCRDLSSSPPGPYGQ CHHHCCCCCCCCCCC | 31.57 | 22167270 | |
| 188 | Ubiquitination | LSSSPPGPYGQEMYA CCCCCCCCCCCCCEE | 35.54 | - | |
| 189 | Phosphorylation | SSSPPGPYGQEMYAF CCCCCCCCCCCCEEE | 37.04 | 21712546 | |
| 194 | Phosphorylation | GPYGQEMYAFRSEER CCCCCCCEEEECHHH | 11.22 | 27794612 | |
| 198 | Phosphorylation | QEMYAFRSEERFKSP CCCEEEECHHHCCCC | 37.04 | 22210691 | |
| 204 | Phosphorylation | RSEERFKSPPILPPH ECHHHCCCCCCCCHH | 32.95 | 113301185 | |
| 249 | Phosphorylation | YALSIKDSVMVLSAT EEEECHHHEEEEECC | 13.70 | 28387310 | |
| 254 | Phosphorylation | KDSVMVLSATHRYKK HHHEEEEECCCCCCC | 21.51 | 28387310 | |
| 256 | Phosphorylation | SVMVLSATHRYKKKY HEEEEECCCCCCCCE | 11.96 | - | |
| 259 | Phosphorylation | VLSATHRYKKKYVTT EEECCCCCCCCEEEE | 21.39 | 28387310 | |
| 263 | Phosphorylation | THRYKKKYVTTLLYK CCCCCCCEEEEEEEC | 16.35 | 28152594 | |
| 265 | Phosphorylation | RYKKKYVTTLLYKPI CCCCCEEEEEEECCC | 14.50 | 26074081 | |
| 266 | Phosphorylation | YKKKYVTTLLYKPI- CCCCEEEEEEECCC- | 12.53 | 26074081 | |
| 269 | Phosphorylation | KYVTTLLYKPI---- CEEEEEEECCC---- | 20.17 | 26074081 | |
| 270 | Ubiquitination | YVTTLLYKPI----- EEEEEEECCC----- | 35.88 | 22505724 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 69 | S | Phosphorylation | Kinase | ULK1 | O75385 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AAKB2_HUMAN !! | ||||||
* 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 AAKB2_HUMAN !! | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-39; SER-108; SER-182;SER-183 AND SER-184, AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY. | |
| "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-39; THR-40 AND SER-184,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-39; SER-108 AND SER-184,AND MASS SPECTROMETRY. | |
| "Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-184, ANDMASS SPECTROMETRY. | |
