UniProt ID | GPB2_YEAST | |
---|---|---|
UniProt AC | P39717 | |
Protein Name | Guanine nucleotide-binding protein subunit beta 2 | |
Gene Name | GPB2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 880 | |
Subcellular Localization | Cytoplasm . Mitochondrion . | |
Protein Description | Beta subunit of a guanine nucleotide-binding protein (G protein). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth.. | |
Protein Sequence | MEISSSPWNDGGYSPYERNRVAVSPFSSALEGEERIETSRSLGDHCFEPLPYVTNYLSIFALFGKEIFGDKGNVSSRNEYLLKKYYSLKKPFVLRHNGHALKNPDMPLQRNDILQTNFMVDKFLNRTVRSVNFNNFKIISDMQSKSGRGTKSGTNQNQSADAIQNICLPSIPSALPYFQYYRKLLTVNTKEWDILKLHSLWVPKLRKDFKDFSLYGDKNSLKPIDSHYDEDNTMKKNLFFERSPSRQTLDGKGCASKGYDISSGNMIIPSLFSEDKLPALTYHCSVELNGNIYIFGGLMPCYSYEEDAPMLNDFFVDGIKNLPPPLLPQVINNPSMVNNPHLYVASIPSCRFSKPKMGGYIPPPLLCVQGSKLTDRHIFFYGGFEIRTETRGDENGKYHLKKRLYVNNTGYILDIMSFKFTKIDIIVQPSKYNAYPTMSSRFGHLQISIDNPNRRASVHSSSMNEIHKMGSASMKQGSSITSGRLEKAAVLSSLPHNTVHTVIIFGGYRQTGDDRYEAMNDLWKIEIPVIRRGKKGYCKFSETANAILLTPSEKDKSDWPEERAFSAFSVHGTSLMDRSSLDMRLLNNLKNHFVLKPSYISQDRVVSPKPVFPMMVHGTHQDLFNSGSAAQESPKAGASASSASAASFDPDMDDNLENYIVNPGRKSSSIPMTAIGRQRLILSQEKPVGKTVVLHGGSNGLNVLDDMWLMDLECETWTPIETFAKADSSEDGDEKLDSVNVGLVGHRMESIGRICVCIGGMVQEDVDQFYSENDDEPPRKRKVDTLPLGGNFLNTIDLSTQCWEEHKITLSKKEDDEDRQDSENEDTNSNIVVGVGGTSLQCDKSIILIGGLISRRSNVKEIYLHGTITKSIFPSVNPSA | |
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 |
---|---|---|---|---|---|
24 | Phosphorylation | ERNRVAVSPFSSALE CCCCEEECCCCHHHC | 15.53 | 22369663 | |
27 | Phosphorylation | RVAVSPFSSALEGEE CEEECCCCHHHCCHH | 20.34 | 22369663 | |
28 | Phosphorylation | VAVSPFSSALEGEER EEECCCCHHHCCHHH | 36.93 | 22369663 | |
213 | Phosphorylation | RKDFKDFSLYGDKNS CCCCCCCCCCCCCCC | 30.71 | 19779198 | |
215 | Phosphorylation | DFKDFSLYGDKNSLK CCCCCCCCCCCCCCC | 23.29 | 19779198 | |
233 | Phosphorylation | SHYDEDNTMKKNLFF CCCCCCCCCCCCEEE | 42.56 | 19779198 | |
243 | Phosphorylation | KNLFFERSPSRQTLD CCEEEECCCCCCCCC | 21.74 | 21440633 | |
245 | Phosphorylation | LFFERSPSRQTLDGK EEEECCCCCCCCCCC | 37.96 | 21440633 | |
248 | Phosphorylation | ERSPSRQTLDGKGCA ECCCCCCCCCCCCCC | 26.21 | 21440633 | |
457 | Phosphorylation | DNPNRRASVHSSSMN CCCCCCEECCCCCHH | 20.67 | 28889911 | |
461 | Phosphorylation | RRASVHSSSMNEIHK CCEECCCCCHHHHHH | 20.80 | 27017623 | |
473 | Phosphorylation | IHKMGSASMKQGSSI HHHHCCCHHCCCCCC | 28.36 | 27017623 | |
481 | Phosphorylation | MKQGSSITSGRLEKA HCCCCCCCCCHHHHH | 27.38 | 27017623 | |
482 | Phosphorylation | KQGSSITSGRLEKAA CCCCCCCCCHHHHHH | 21.90 | 27017623 | |
601 | Phosphorylation | VLKPSYISQDRVVSP EECHHHCCCCCCCCC | 20.14 | 27717283 | |
607 | Phosphorylation | ISQDRVVSPKPVFPM CCCCCCCCCCCCCCE | 25.09 | 21551504 | |
628 | Phosphorylation | QDLFNSGSAAQESPK HHHHHCCCCCCCCCC | 21.91 | 24961812 | |
633 | Phosphorylation | SGSAAQESPKAGASA CCCCCCCCCCCCCCC | 21.44 | 20377248 | |
644 | Phosphorylation | GASASSASAASFDPD CCCCCCHHHHHCCCC | 26.73 | 21551504 | |
647 | Phosphorylation | ASSASAASFDPDMDD CCCHHHHHCCCCCCC | 29.87 | 21551504 | |
668 | Phosphorylation | VNPGRKSSSIPMTAI CCCCCCCCCCCCCHH | 35.01 | 23749301 | |
669 | Phosphorylation | NPGRKSSSIPMTAIG CCCCCCCCCCCCHHC | 37.49 | 19779198 | |
673 | Phosphorylation | KSSSIPMTAIGRQRL CCCCCCCCHHCCCEE | 15.12 | 28889911 | |
686 | Ubiquitination | RLILSQEKPVGKTVV EEEEECCCCCCCEEE | 37.05 | 23749301 |
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 GPB2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GPB2_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 GPB2_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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-24, AND MASSSPECTROMETRY. |