| UniProt ID | GNAS2_MOUSE | |
|---|---|---|
| UniProt AC | P63094 | |
| Protein Name | Guanine nucleotide-binding protein G(s) subunit alpha isoforms short | |
| Gene Name | Gnas | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 394 | |
| Subcellular Localization |
Cell membrane Lipid-anchor . |
|
| Protein Description | Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP. GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. Stimulates the Ras signaling pathway via RAPGEF2.. | |
| Protein Sequence | MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPNFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL | |
| 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-palmitoylation | ------MGCLGNSKT ------CCCCCCCCC | 18.50 | - | |
| 3 | S-palmitoylation | -----MGCLGNSKTE -----CCCCCCCCCH | 4.20 | 8227063 | |
| 8 | Ubiquitination | MGCLGNSKTEDQRNE CCCCCCCCCHHHHHH | 60.99 | 22790023 | |
| 17 | Ubiquitination | EDQRNEEKAQREANK HHHHHHHHHHHHHHH | 43.57 | 22790023 | |
| 51 | Phosphorylation | LLLGAGESGKSTIVK HHHCCCCCCCCHHHE | 51.07 | 27841257 | |
| 51 (in isoform 2) | Phosphorylation | - | 51.07 | 27841257 | |
| 53 | Ubiquitination | LGAGESGKSTIVKQM HCCCCCCCCHHHEEE | 54.42 | - | |
| 58 | Ubiquitination | SGKSTIVKQMRILHV CCCCHHHEEEEEEEE | 34.23 | 22790023 | |
| 58 | Acetylation | SGKSTIVKQMRILHV CCCCHHHEEEEEEEE | 34.23 | 22826441 | |
| 96 | Ubiquitination | ATKVQDIKNNLKEAI CHHHHHHHHHHHHHH | 48.34 | 22790023 | |
| 100 | Ubiquitination | QDIKNNLKEAIETIV HHHHHHHHHHHHHHH | 47.42 | - | |
| 177 | Phosphorylation | QLIDCAQYFLDKIDV EEHHHHHHHHHHCHH | 6.38 | - | |
| 181 | Ubiquitination | CAQYFLDKIDVIKQA HHHHHHHHCHHHHHC | 42.84 | - | |
| 186 | Ubiquitination | LDKIDVIKQADYVPS HHHCHHHHHCCCCCC | 39.00 | 22790023 | |
| 205 | Phosphorylation | LRCRVLTSGIFETKF HHHEEECCCCCEEEE | 26.23 | - | |
| 211 | Ubiquitination | TSGIFETKFQVDKVN CCCCCEEEEEEEEEE | 26.97 | 22790023 | |
| 216 | Ubiquitination | ETKFQVDKVNFHMFD EEEEEEEEEEEEEEE | 39.97 | 22790023 | |
| 274 | Ubiquitination | QEALNLFKSIWNNRW HHHHHHHHHHHCCHH | 44.17 | - | |
| 300 | Ubiquitination | KQDLLAEKVLAGKSK HHHHHHHHHHCCCHH | 36.62 | 22790023 | |
| 307 | Ubiquitination | KVLAGKSKIEDYFPE HHHCCCHHHHHHCHH | 54.31 | 22790023 | |
| 311 | Phosphorylation | GKSKIEDYFPEFARY CCHHHHHHCHHHHCC | 14.29 | - | |
| 320 | Phosphorylation | PEFARYTTPEDATPE HHHHCCCCCCCCCCC | 18.75 | - | |
| 338 | Ubiquitination | DPRVTRAKYFIRDEF CCCCCEEEEEECCCH | 37.09 | 22790023 | |
| 350 | Phosphorylation | DEFLRISTASGDGRH CCHHEEEECCCCCCC | 23.59 | - | |
| 352 | Phosphorylation | FLRISTASGDGRHYC HHEEEECCCCCCCCE | 37.19 | - | |
| 360 | Phosphorylation | GDGRHYCYPHFTCAV CCCCCCEECCEEEEE | 7.80 | - | |
| 365 | S-palmitoylation | YCYPHFTCAVDTENI CEECCEEEEECHHHH | 3.21 | 28680068 |
| 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 GNAS2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GNAS2_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 GNAS2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GNAS2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Palmitoylation | |
| Reference | PubMed |
| "Palmitoylation is required for signaling functions and membraneattachment of Gq alpha and Gs alpha."; Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R.; J. Biol. Chem. 268:25001-25008(1993). Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-3, AND MUTAGENESIS OFCYS-3. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY. | |
