| UniProt ID | SH3G2_HUMAN | |
|---|---|---|
| UniProt AC | Q99962 | |
| Protein Name | Endophilin-A1 | |
| Gene Name | SH3GL2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 352 | |
| Subcellular Localization |
Cytoplasm . Membrane Peripheral membrane protein . Early endosome . Concentrated in presynaptic nerve terminals in neurons. |
|
| Protein Description | Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes.. | |
| Protein Sequence | MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFPTGDSTQPNGGLSHTGTPKPSGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGHSGFFPINYVEILVALPH | |
| 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 | Phosphorylation | ------MSVAGLKKQ ------CCHHHHHHH | 22.22 | 29514088 | |
| 14 | Phosphorylation | KKQFHKATQKVSEKV HHHHHHHHHHHHHHH | 33.45 | 22817900 | |
| 54 | Phosphorylation | VMEIMTKTIEYLQPN HHHHHHHHHHHHCCC | 15.18 | 28152594 | |
| 57 | Phosphorylation | IMTKTIEYLQPNPAS HHHHHHHHHCCCHHH | 13.54 | 28152594 | |
| 64 | Phosphorylation | YLQPNPASRAKLSMI HHCCCHHHHHHHHHH | 33.75 | 28152594 | |
| 75 | Phosphorylation | LSMINTMSKIRGQEK HHHHHHHHHHCCCCC | 23.92 | 22817900 | |
| 76 | Acetylation | SMINTMSKIRGQEKG HHHHHHHHHCCCCCC | 26.12 | 19812095 | |
| 86 | Phosphorylation | GQEKGPGYPQAEALL CCCCCCCCHHHHHHH | 8.70 | 22817900 | |
| 149 | Ubiquitination | PLQNLHDKDLREIQH HHHHCCHHHHHHHHH | 48.17 | - | |
| 159 | Ubiquitination | REIQHHLKKLEGRRL HHHHHHHHHHCCCCC | 51.46 | - | |
| 177 | Ubiquitination | YKKKRQGKIPDEELR HHHHHCCCCCHHHHH | 42.60 | - | |
| 184 | Methylation | KIPDEELRQALEKFD CCCHHHHHHHHHHHH | 24.01 | - | |
| 237 | Phosphorylation | VQILQQVTVRLEERI HHHHHHHHHHHHHHH | 8.79 | 24719451 | |
| 249 | Phosphorylation | ERIRQASSQPRREYQ HHHHHHHCCCCCCCC | 47.41 | 22617229 | |
| 262 | Phosphorylation | YQPKPRMSLEFPTGD CCCCCCEEEECCCCC | 26.48 | 29449344 | |
| 267 | Phosphorylation | RMSLEFPTGDSTQPN CEEEECCCCCCCCCC | 59.97 | 29449344 | |
| 270 | Phosphorylation | LEFPTGDSTQPNGGL EECCCCCCCCCCCCC | 30.22 | 29449344 | |
| 271 | Phosphorylation | EFPTGDSTQPNGGLS ECCCCCCCCCCCCCC | 53.43 | 24719451 | |
| 278 | Phosphorylation | TQPNGGLSHTGTPKP CCCCCCCCCCCCCCC | 23.44 | 24719451 | |
| 280 | Phosphorylation | PNGGLSHTGTPKPSG CCCCCCCCCCCCCCC | 39.10 | 25627689 | |
| 282 | Phosphorylation | GGLSHTGTPKPSGVQ CCCCCCCCCCCCCCC | 29.33 | 25627689 | |
| 299 | Phosphorylation | QPCCRALYDFEPENE CCCEEECCCCCCCCC | 20.01 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SH3G2_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 SH3G2_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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| Phosphorylation | |
| Reference | PubMed |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY. | |