| UniProt ID | SIP2_YEAST | |
|---|---|---|
| UniProt AC | P34164 | |
| Protein Name | SNF1 protein kinase subunit beta-2 | |
| Gene Name | SIP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 415 | |
| Subcellular Localization |
Cytoplasm . Cell membrane Peripheral membrane protein Cytoplasmic side . Resides in the cytosol during growth in glucose. Excluded from the nucleus. There is an age-associated shift in localization from the plasma membrane to the cytoplasm. |
|
| Protein Description | Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.. | |
| Protein Sequence | MGTTTSHPAQKKQTTKKCRAPIMSDVREKPSNAQGCEPQEMDAVSKKVTELSLNKCSDSQDAGQPSREGSITKKKSTLLLRDEDEPTMPKLSVMETAVDTDSGSSSTSDDEEGDIIAQTTEPKQDASPDDDRSGHSSPREEGQQQIRAKEASGGPSEIKSSLMVPVEIRWQQGGSKVYVTGSFTKWRKMIGLIPDSDNNGSFHVKLRLLPGTHRFRFIVDNELRVSDFLPTATDQMGNFVNYIEVRQPEKNPTNEKIRSKEADSMRPPTSDRSSIALQIGKDPDDFGDGYTRFHEDLSPRPPLEYTTDIPAVFTDPSVMERYYYTLDRQQSNTDTSWLTPPQLPPQLENVILNKYYATQDQFNENNSGALPIPNHVVLNHLVTSSIKHNTLCVASIVRYKQKYVTQILYTPIESS | |
| 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 |
|---|---|---|---|---|---|
| 2 | N-myristoyl glycine | ------MGTTTSHPA ------CCCCCCCHH | 31.59 | - | |
| 2 | Myristoylation | ------MGTTTSHPA ------CCCCCCCHH | 31.59 | 12562756 | |
| 3 | Phosphorylation | -----MGTTTSHPAQ -----CCCCCCCHHH | 26.12 | 28889911 | |
| 4 | Phosphorylation | ----MGTTTSHPAQK ----CCCCCCCHHHH | 22.14 | 30377154 | |
| 5 | Phosphorylation | ---MGTTTSHPAQKK ---CCCCCCCHHHHC | 25.52 | 30377154 | |
| 6 | Phosphorylation | --MGTTTSHPAQKKQ --CCCCCCCHHHHCC | 25.94 | 30377154 | |
| 12 | Acetylation | TSHPAQKKQTTKKCR CCCHHHHCCCCCCCC | 40.57 | 21906795 | |
| 16 | Acetylation | AQKKQTTKKCRAPIM HHHCCCCCCCCCCCC | 53.95 | 21906795 | |
| 17 | Acetylation | QKKQTTKKCRAPIMS HHCCCCCCCCCCCCH | 27.19 | 21906795 | |
| 29 | Ubiquitination | IMSDVREKPSNAQGC CCHHHCCCCCCCCCC | 43.09 | 23749301 | |
| 45 | Phosphorylation | PQEMDAVSKKVTELS HHHHHHHHHHHHHHH | 28.60 | 21551504 | |
| 49 | Phosphorylation | DAVSKKVTELSLNKC HHHHHHHHHHHHHCC | 39.84 | 22369663 | |
| 52 | Phosphorylation | SKKVTELSLNKCSDS HHHHHHHHHHCCCCC | 24.54 | 22369663 | |
| 55 | Ubiquitination | VTELSLNKCSDSQDA HHHHHHHCCCCCCCC | 40.17 | 23749301 | |
| 57 | Phosphorylation | ELSLNKCSDSQDAGQ HHHHHCCCCCCCCCC | 41.74 | 22369663 | |
| 59 | Phosphorylation | SLNKCSDSQDAGQPS HHHCCCCCCCCCCCC | 17.42 | 22369663 | |
| 66 | Phosphorylation | SQDAGQPSREGSITK CCCCCCCCCCCCCCC | 34.77 | 22369663 | |
| 70 | Phosphorylation | GQPSREGSITKKKST CCCCCCCCCCCCEEE | 23.49 | 22369663 | |
| 72 | Phosphorylation | PSREGSITKKKSTLL CCCCCCCCCCEEEEE | 38.21 | 22369663 | |
| 76 | Phosphorylation | GSITKKKSTLLLRDE CCCCCCEEEEEECCC | 32.92 | 22369663 | |
| 77 | Phosphorylation | SITKKKSTLLLRDED CCCCCEEEEEECCCC | 30.24 | 22369663 | |
| 87 | Phosphorylation | LRDEDEPTMPKLSVM ECCCCCCCCCCEEEE | 44.02 | 22369663 | |
| 127 | Phosphorylation | TEPKQDASPDDDRSG CCCCCCCCCCCCCCC | 36.83 | 29136822 | |
| 133 | Phosphorylation | ASPDDDRSGHSSPRE CCCCCCCCCCCCCCH | 48.10 | 17563356 | |
| 136 | Phosphorylation | DDDRSGHSSPREEGQ CCCCCCCCCCCHHHH | 45.63 | 29136822 | |
| 137 | Phosphorylation | DDRSGHSSPREEGQQ CCCCCCCCCCHHHHH | 23.46 | 17563356 | |
| 152 | Phosphorylation | QIRAKEASGGPSEIK HHHHHHHCCCCCCCC | 45.43 | 25752575 | |
| 160 | Phosphorylation | GGPSEIKSSLMVPVE CCCCCCCCEEEEEEE | 34.07 | 22369663 | |
| 161 | Phosphorylation | GPSEIKSSLMVPVEI CCCCCCCEEEEEEEE | 18.58 | 22369663 | |
| 182 | Phosphorylation | SKVYVTGSFTKWRKM CEEEEEECCCCHHHE | 22.00 | 27214570 | |
| 256 | Acetylation | EKNPTNEKIRSKEAD CCCCCCHHHCHHHHH | 45.55 | 21906795 | |
| 273 | Phosphorylation | RPPTSDRSSIALQIG CCCCCCCHHEEHHCC | 30.96 | 28889911 | |
| 274 | Phosphorylation | PPTSDRSSIALQIGK CCCCCCHHEEHHCCC | 16.87 | 28889911 | |
| 298 | Phosphorylation | TRFHEDLSPRPPLEY CCCCCCCCCCCCCCC | 31.05 | 12562756 | |
| 305 | Phosphorylation | SPRPPLEYTTDIPAV CCCCCCCCCCCCCCC | 23.71 | 19779198 | |
| 306 | Phosphorylation | PRPPLEYTTDIPAVF CCCCCCCCCCCCCCC | 14.49 | 19779198 | |
| 307 | Phosphorylation | RPPLEYTTDIPAVFT CCCCCCCCCCCCCCC | 30.91 | 19779198 | |
| 331 | Phosphorylation | YTLDRQQSNTDTSWL EECCCCCCCCCCCCC | 33.10 | 30377154 | |
| 354 | Ubiquitination | LENVILNKYYATQDQ HHHHHHHHHCCCHHH | 35.87 | 17644757 |
| 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 SIP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIP2_YEAST !! | ||||||
* 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 SIP2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Myristoylation | |
| Reference | PubMed |
| "Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates agingin Saccharomyces cerevisiae by affecting cellular histone kinaseactivity, recombination at rDNA loci, and silencing."; Lin S.S., Manchester J.K., Gordon J.I.; J. Biol. Chem. 278:13390-13397(2003). Cited for: FUNCTION, MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF GLY-2. | |
| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND THR-72, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-52; SER-133 ANDSER-137, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND THR-77, AND MASSSPECTROMETRY. | |
