UniProt ID | SEC62_YEAST | |
---|---|---|
UniProt AC | P21825 | |
Protein Name | Translocation protein SEC62 | |
Gene Name | SEC62 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 274 | |
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 KAR2 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 SEC1-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. SEC62 is essential for cell growth.. | |
Protein Sequence | MSAVGPGSNAGASVNGGSATAIATLLRNHKELKQRQGLFQAKQTDFFRYKRFVRALHSEEYANKSARQPEIYPTIPSNKIEDQLKSREIFIQLIKAQMVIPVKKLHSQECKEHGLKPSKDFPHLIVSNKAQLEADEYFVWNYNPRTYMDYLIVIGVVSIILALVCYPLWPRSMRRGSYYVSLGAFGILAGFFAVAILRLILYVLSLIVYKDVGGFWIFPNLFEDCGVLESFKPLYGFGEKDTYSYKKKLKRMKKKQAKRESNKKKAINEKAEQN | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MSAVGPGSN ------CCCCCCCCC | 31.49 | 22814378 | |
2 | Phosphorylation | ------MSAVGPGSN ------CCCCCCCCC | 31.49 | 22369663 | |
8 | Phosphorylation | MSAVGPGSNAGASVN CCCCCCCCCCCCCCC | 27.00 | 28132839 | |
13 | Phosphorylation | PGSNAGASVNGGSAT CCCCCCCCCCHHHHH | 18.39 | 28132839 | |
18 | Phosphorylation | GASVNGGSATAIATL CCCCCHHHHHHHHHH | 24.68 | 28132839 | |
20 | Phosphorylation | SVNGGSATAIATLLR CCCHHHHHHHHHHHH | 21.94 | 28132839 | |
24 | Phosphorylation | GSATAIATLLRNHKE HHHHHHHHHHHCHHH | 21.88 | 28132839 | |
79 | Acetylation | YPTIPSNKIEDQLKS CCCCCCCHHHHHHHH | 52.38 | 24489116 | |
116 | Acetylation | ECKEHGLKPSKDFPH HHHHCCCCCCCCCCE | 52.41 | 24489116 | |
119 | Acetylation | EHGLKPSKDFPHLIV HCCCCCCCCCCEEEE | 72.43 | 24489116 | |
242 | Phosphorylation | YGFGEKDTYSYKKKL CCCCCCCCCHHHHHH | 25.99 | 27017623 | |
243 | Phosphorylation | GFGEKDTYSYKKKLK CCCCCCCCHHHHHHH | 21.82 | 27017623 | |
245 | Phosphorylation | GEKDTYSYKKKLKRM CCCCCCHHHHHHHHH | 19.20 | 27017623 | |
270 | Ubiquitination | KKKAINEKAEQN--- HHHHHHHHHHHC--- | 53.38 | 23749301 |
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_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC62_YEAST !! |
* 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_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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