| UniProt ID | STAM2_MOUSE | |
|---|---|---|
| UniProt AC | O88811 | |
| Protein Name | Signal transducing adapter molecule 2 | |
| Gene Name | Stam2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 523 | |
| Subcellular Localization |
Cytoplasm . Early endosome membrane Peripheral membrane protein Cytoplasmic side. |
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| Protein Description | Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity).. | |
| Protein Sequence | MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDRVGSTPSGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRSVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGVTFPSAGSQTVAAAAKNGTSLNKNKEDEDIAKAIELSLQEQKQQYTETKALYPPAESQLNNKAARRVRALYDFEAVEDNELTFKHGELITVLDDSDANWWQGENHRGTGLFPSNFVTTDLSTEVETATVDKLNVIDDDVEEIKKSEPEPVYIDEGKMDRALQILQSIDPKESKPDSQDLLDLEDVCQQMGPMIDEKLEEIDRKHSELSELNVKVLEALDLYNKLVNEAPVYSVYSKLHPAHYPPAAAGVPVQTYPVQSHGGNYLGHGIHQVSVAQNYNLGPDPMGSLRSLPPNMNSVTAHTVQPPYLSTGQDTVSNPSYMNQSSRLQAAAGTAAYTQPVGMSTDVSSFQNTASGLPQLAGFPVAVPAPVAAQPQASYHQQPLL | |
| 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 |
|---|---|---|---|---|---|
| 134 | Ubiquitination | SLISATIKSMKEEGV HHHHHHHHHHHHHCC | 39.89 | 22790023 | |
| 156 | Ubiquitination | QTVAAAAKNGTSLNK HHHHHHHHCCCCCCC | 51.70 | 22790023 | |
| 182 | Ubiquitination | ELSLQEQKQQYTETK HHHHHHHHHHHHHHH | 38.32 | 22790023 | |
| 185 | Phosphorylation | LQEQKQQYTETKALY HHHHHHHHHHHHCCC | 12.21 | 29514104 | |
| 189 | Ubiquitination | KQQYTETKALYPPAE HHHHHHHHCCCCCHH | 30.11 | 22790023 | |
| 192 | Phosphorylation | YTETKALYPPAESQL HHHHHCCCCCHHHHH | 16.42 | 26026062 | |
| 202 | Ubiquitination | AESQLNNKAARRVRA HHHHHCHHHHHHHHH | 42.20 | 22790023 | |
| 284 | Ubiquitination | DDVEEIKKSEPEPVY CCHHHHHHCCCCCEE | 66.76 | 22790023 | |
| 285 | Phosphorylation | DVEEIKKSEPEPVYI CHHHHHHCCCCCEEE | 54.07 | 25338131 | |
| 343 | Ubiquitination | KLEEIDRKHSELSEL HHHHHHHHCHHHHHH | 47.97 | - | |
| 363 | Ubiquitination | EALDLYNKLVNEAPV HHHHHHHHHHCCCCC | 40.01 | - | |
| 371 | Phosphorylation | LVNEAPVYSVYSKLH HHCCCCCHHHCCCCC | 7.43 | 26032504 | |
| 372 | Phosphorylation | VNEAPVYSVYSKLHP HCCCCCHHHCCCCCC | 18.14 | 25367039 | |
| 374 | Phosphorylation | EAPVYSVYSKLHPAH CCCCHHHCCCCCCCC | 8.31 | 20116462 | |
| 375 | Phosphorylation | APVYSVYSKLHPAHY CCCHHHCCCCCCCCC | 26.95 | 22817900 |
| 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 STAM2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STAM2_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 STAM2_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374, AND MASSSPECTROMETRY. | |