UniProt ID | SEC62_SCHPO | |
---|---|---|
UniProt AC | O13787 | |
Protein Name | Translocation protein sec62 | |
Gene Name | sec62 | |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
Sequence Length | 273 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
Protein Description | Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to sec61 and sec62. sec62 and sec63 are required for interactions between sec61 and translocating polypeptides. sec62 may affect sec61-polypeptide interactions by increasing the affinity of targeting pathways for sec61 and/or by modifying sec61 to allow more efficient polypeptide interaction. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon (By similarity).. | |
Protein Sequence | MDSSNVPVLKDEDKCKFSMRFTNFLKSRPELKTKPAILNGKRVYYFRVKRVLRFLTSEAYTPKKYKGFPEISSREEAIEVLKLLIMNSMLVRVDKLPPKQRKQKLVELQINRNQDFQDDMHYVWLYEPLPKRVMALAVLFALVVLALVLFPLWPMFMRKGAWYLSMGGLGVIGLFFVLVILRFFLFCITAVIVRPGIWLFPNLLADVGFCDSFKPLWSWHNSKSEVKKTRKSKKLSKKATSPAASATPEKSSTSTTSLKNLRHRNPTVEEVSE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
240 | Phosphorylation | KKLSKKATSPAASAT HHHHHHCCCCCCCCC | 44.09 | 25720772 | |
241 | Phosphorylation | KLSKKATSPAASATP HHHHHCCCCCCCCCC | 19.87 | 24763107 | |
245 | Phosphorylation | KATSPAASATPEKSS HCCCCCCCCCCCCCC | 34.48 | 29996109 | |
247 | Phosphorylation | TSPAASATPEKSSTS CCCCCCCCCCCCCCC | 29.50 | 25720772 | |
251 | Phosphorylation | ASATPEKSSTSTTSL CCCCCCCCCCCCCCH | 36.87 | 29996109 | |
253 | Phosphorylation | ATPEKSSTSTTSLKN CCCCCCCCCCCCHHH | 36.86 | 25720772 | |
254 | Phosphorylation | TPEKSSTSTTSLKNL CCCCCCCCCCCHHHH | 31.47 | 29996109 | |
255 | Phosphorylation | PEKSSTSTTSLKNLR CCCCCCCCCCHHHHH | 22.09 | 29996109 | |
256 | Phosphorylation | EKSSTSTTSLKNLRH CCCCCCCCCHHHHHH | 31.65 | 29996109 | |
257 | Phosphorylation | KSSTSTTSLKNLRHR CCCCCCCCHHHHHHC | 37.12 | 29996109 | |
267 | Phosphorylation | NLRHRNPTVEEVSE- HHHHCCCCHHHHCC- | 44.06 | 21712547 | |
272 | Phosphorylation | NPTVEEVSE------ CCCHHHHCC------ | 40.65 | 19547744 |
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 SEC62_SCHPO !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC62_SCHPO !! |
* 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 SEC62_SCHPO !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SAD1_SCHPO | sad1 | physical | 23695164 | |
SWS1_SCHPO | sws1 | physical | 26771498 | |
SAD1_SCHPO | sad1 | physical | 26771498 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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