| UniProt ID | RGS2_HUMAN | |
|---|---|---|
| UniProt AC | P41220 | |
| Protein Name | Regulator of G-protein signaling 2 | |
| Gene Name | RGS2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 211 | |
| Subcellular Localization |
Isoform 1: Cell membrane . Cytoplasm . Nucleus, nucleolus . Isoform 2: Cell membrane . Cytoplasm . Nucleus, nucleolus . Isoform 3: Cell membrane . Cytoplasm . Nucleus, nucleolus . Isoform 4: Cell membrane . Mitochondrion . |
|
| Protein Description | Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. [PubMed: 11063746] | |
| Protein Sequence | MQSAMFLAVQHDCRPMDKSAGSGHKSEEKREKMKRTLLKDWKTRLSYFLQNSSTPGKPKTGKKSKQQAFIKPSPEEAQLWSEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCKKPQITTEPHAT | |
| 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 |
|---|---|---|---|---|---|
| 39 | Ubiquitination | KMKRTLLKDWKTRLS HHHHHHHHHHHHHHH | 65.73 | - | |
| 46 | Phosphorylation | KDWKTRLSYFLQNSS HHHHHHHHHHHHCCC | 15.56 | 14608379 | |
| 47 | Phosphorylation | DWKTRLSYFLQNSST HHHHHHHHHHHCCCC | 16.95 | 24719451 | |
| 52 | Phosphorylation | LSYFLQNSSTPGKPK HHHHHHCCCCCCCCC | 23.72 | 28555341 | |
| 53 | Phosphorylation | SYFLQNSSTPGKPKT HHHHHCCCCCCCCCC | 46.28 | 24719451 | |
| 54 | Phosphorylation | YFLQNSSTPGKPKTG HHHHCCCCCCCCCCC | 35.56 | 28555341 | |
| 57 | Ubiquitination | QNSSTPGKPKTGKKS HCCCCCCCCCCCCCC | 44.54 | - | |
| 64 | Phosphorylation | KPKTGKKSKQQAFIK CCCCCCCCCCEECCC | 38.90 | 14608379 | |
| 71 | Ubiquitination | SKQQAFIKPSPEEAQ CCCEECCCCCHHHHH | 32.75 | - | |
| 106 | S-palmitoylation | AFLKSEFCEENIEFW HHHHHHHHHHHHHHH | 5.87 | 16945566 | |
| 116 | S-palmitoylation | NIEFWLACEDFKKTK HHHHHHHCHHHHCCC | 4.89 | 16945566 | |
| 121 | Acetylation | LACEDFKKTKSPQKL HHCHHHHCCCCHHHH | 62.27 | 12654859 | |
| 123 | Acetylation | CEDFKKTKSPQKLSS CHHHHCCCCHHHHHH | 69.85 | 12654869 | |
| 127 | Ubiquitination | KKTKSPQKLSSKARK HCCCCHHHHHHHHHH | 54.44 | - | |
| 134 | Ubiquitination | KLSSKARKIYTDFIE HHHHHHHHHHHHHHH | 44.94 | - | |
| 142 | Ubiquitination | IYTDFIEKEAPKEIN HHHHHHHHHCCCCCC | 55.12 | - | |
| 146 | Ubiquitination | FIEKEAPKEINIDFQ HHHHHCCCCCCCCHH | 77.57 | - | |
| 156 | Phosphorylation | NIDFQTKTLIAQNIQ CCCHHHHHHHHHHHH | 27.12 | 28985074 | |
| 167 | Phosphorylation | QNIQEATSGCFTTAQ HHHHHHHCCCCHHHH | 40.38 | 28985074 | |
| 171 | Phosphorylation | EATSGCFTTAQKRVY HHHCCCCHHHHHHHH | 25.87 | 28985074 | |
| 172 | Phosphorylation | ATSGCFTTAQKRVYS HHCCCCHHHHHHHHH | 13.57 | 28985074 | |
| 175 | Ubiquitination | GCFTTAQKRVYSLME CCCHHHHHHHHHHHH | 41.17 | - | |
| 178 | Phosphorylation | TTAQKRVYSLMENNS HHHHHHHHHHHHCCC | 10.50 | 30257219 | |
| 179 | Phosphorylation | TAQKRVYSLMENNSY HHHHHHHHHHHCCCC | 20.55 | - | |
| 186 | Phosphorylation | SLMENNSYPRFLESE HHHHCCCCCCHHHHH | 10.68 | 30257219 | |
| 195 | Phosphorylation | RFLESEFYQDLCKKP CHHHHHHHHHHHCCC | 9.32 | 27642862 | |
| 199 | S-palmitoylation | SEFYQDLCKKPQITT HHHHHHHHCCCCCCC | 7.77 | 16945566 | |
| 201 | Ubiquitination | FYQDLCKKPQITTEP HHHHHHCCCCCCCCC | 40.95 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RGS2_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 RGS2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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