| UniProt ID | G3BP2_MOUSE | |
|---|---|---|
| UniProt AC | P97379 | |
| Protein Name | Ras GTPase-activating protein-binding protein 2 | |
| Gene Name | G3bp2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 482 | |
| Subcellular Localization | ||
| Protein Description | Probable scaffold protein that may be involved in mRNA transport.. | |
| Protein Sequence | MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEDRQPSPEPVQENANSAYYDAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKHLEELEEKSATPPPAEPASLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVDAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMTQKLGSGRGTGQMEGRFTGQRR | |
| 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 |
|---|---|---|---|---|---|
| 5 | Ubiquitination | ---MVMEKPSPLLVG ---CCCCCCCCCEEC | 32.47 | - | |
| 7 | Phosphorylation | -MVMEKPSPLLVGRE -CCCCCCCCCEECHH | 38.97 | 30482847 | |
| 25 | Ubiquitination | QYYTLLNKAPEYLHR HHHHHHHHCHHHHHH | 66.35 | - | |
| 38 | Phosphorylation | HRFYGRNSSYVHGGV HHHHCCCCCCCCCCC | 22.99 | 25367039 | |
| 39 | Phosphorylation | RFYGRNSSYVHGGVD HHHCCCCCCCCCCCC | 34.42 | 25367039 | |
| 40 | Phosphorylation | FYGRNSSYVHGGVDA HHCCCCCCCCCCCCC | 9.04 | 25367039 | |
| 48 | Phosphorylation | VHGGVDASGKPQEAV CCCCCCCCCCCCCCC | 42.77 | 25367039 | |
| 56 | Phosphorylation | GKPQEAVYGQNDIHH CCCCCCCCCCCCHHH | 21.75 | 18563927 | |
| 73 | S-nitrosocysteine | LSLNFSECHTKIRHV EEECHHHHCCEEEEE | 4.84 | - | |
| 73 | S-nitrosylation | LSLNFSECHTKIRHV EEECHHHHCCEEEEE | 4.84 | 20925432 | |
| 73 | S-palmitoylation | LSLNFSECHTKIRHV EEECHHHHCCEEEEE | 4.84 | 26165157 | |
| 107 | Acetylation | NSGQPERKFMQTFVL CCCCCCHHEEEEEEE | 43.45 | 22826441 | |
| 107 | Ubiquitination | NSGQPERKFMQTFVL CCCCCCHHEEEEEEE | 43.45 | - | |
| 133 | Phosphorylation | VHNDMFRYEDEVFGD EECCCEECCCCCCCC | 19.23 | 29550500 | |
| 141 | Phosphorylation | EDEVFGDSEPELDEE CCCCCCCCCCCCCCC | 56.27 | 25521595 | |
| 149 | Phosphorylation | EPELDEESEDEVEEE CCCCCCCCHHHHHHH | 48.58 | 25521595 | |
| 163 | Phosphorylation | EQEDRQPSPEPVQEN HHHHCCCCCCCCHHC | 33.29 | 25521595 | |
| 206 | Phosphorylation | EPESETKTEELKPQV CCCCCCCHHHHHHHH | 41.95 | 28973931 | |
| 225 | Phosphorylation | LEELEEKSATPPPAE HHHHHHHCCCCCCCC | 40.43 | 27087446 | |
| 225 (in isoform 2) | Phosphorylation | - | 40.43 | 25521595 | |
| 227 | Phosphorylation | ELEEKSATPPPAEPA HHHHHCCCCCCCCCC | 43.34 | 27087446 | |
| 227 (in isoform 2) | Phosphorylation | - | 43.34 | 25521595 | |
| 235 (in isoform 2) | Phosphorylation | - | 51.83 | 26239621 | |
| 235 | Phosphorylation | PPPAEPASLPQEPPK CCCCCCCCCCCCCCC | 51.83 | 25521595 | |
| 235 | O-linked_Glycosylation | PPPAEPASLPQEPPK CCCCCCCCCCCCCCC | 51.83 | 22517741 | |
| 245 | Phosphorylation | QEPPKAFSWASVTSK CCCCCCCCCEECCCC | 26.96 | 23140645 | |
| 250 | Phosphorylation | AFSWASVTSKNLPPS CCCCEECCCCCCCCC | 31.33 | 20469934 | |
| 251 | Phosphorylation | FSWASVTSKNLPPSG CCCEECCCCCCCCCC | 19.86 | 20469934 | |
| 281 | Ubiquitination | SQPRVDAKPEVQSQP CCCCCCCCCCHHCCC | 36.93 | - | |
| 281 | Malonylation | SQPRVDAKPEVQSQP CCCCCCCCCCHHCCC | 36.93 | 26320211 | |
| 327 | Phosphorylation | DNRRIIRYPDSHQLF CCCEEEECCCCCCEE | 10.86 | 29899451 | |
| 330 | Phosphorylation | RIIRYPDSHQLFVGN EEEECCCCCCEEECC | 14.50 | 29899451 | |
| 370 | Ubiquitination | NTKGVGGKLPNFGFV ECCCCCCCCCCCEEE | 55.64 | - | |
| 392 | Succinylation | VQRILIAKPIMFRGE HHEEEEEECEEECCE | 28.25 | - | |
| 392 | Acetylation | VQRILIAKPIMFRGE HHEEEEEECEEECCE | 28.25 | 23806337 | |
| 392 | Malonylation | VQRILIAKPIMFRGE HHEEEEEECEEECCE | 28.25 | 32601280 | |
| 392 | Succinylation | VQRILIAKPIMFRGE HHEEEEEECEEECCE | 28.25 | 23806337 | |
| 457 | Methylation | DGRGPPPRGGMTQKL CCCCCCCCCCCEEEC | 61.13 | - | |
| 457 | Dimethylation | DGRGPPPRGGMTQKL CCCCCCCCCCCEEEC | 61.13 | - | |
| 466 | Phosphorylation | GMTQKLGSGRGTGQM CCEEECCCCCCCCCC | 35.44 | - | |
| 468 | Methylation | TQKLGSGRGTGQMEG EEECCCCCCCCCCCC | 40.99 | 24129315 | |
| 468 | Dimethylation | TQKLGSGRGTGQMEG EEECCCCCCCCCCCC | 40.99 | - |
| 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 G3BP2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of G3BP2_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 G3BP2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of G3BP2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND THR-227, ANDMASS SPECTROMETRY. | |
| "Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND MASSSPECTROMETRY. | |
| "Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND MASSSPECTROMETRY. | |