| UniProt ID | SEC65_YEAST | |
|---|---|---|
| UniProt AC | P29478 | |
| Protein Name | Signal recognition particle subunit SEC65 | |
| Gene Name | SEC65 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 273 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SEC65 is required for SRP integrity.. | |
| Protein Sequence | MPRLEEIDDFNDIDDLDMELAELDPSLRTPIAPKITPKVVRSQDQENPAFLPGTNNNSNSNNNSSNEKEQLSFINPKTGKVERSEAISKKDLEEVKRFQVLYPCYFDINRSHKEGRRVPKELAVENPLAKTMADAVRELGILCIFEGEKCHPQDFGNPGRIRVLFKENGQLIGAATKFKGGKRQLMKAVGEYMKRHPTTIESLREIPYGPDFDNIEFKKIPRVKGFKMNEIVPLHSPFLMGHPMTKSVYETPKITAAEKSFKPPKNKYKVVRR | |
| 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 |
|---|---|---|---|---|---|
| 26 | Phosphorylation | ELAELDPSLRTPIAP HHHHHCHHHCCCCCC | 30.10 | 22369663 | |
| 29 | Phosphorylation | ELDPSLRTPIAPKIT HHCHHHCCCCCCCCC | 25.08 | 22369663 | |
| 34 | Acetylation | LRTPIAPKITPKVVR HCCCCCCCCCHHHCC | 50.63 | 25381059 | |
| 36 | Phosphorylation | TPIAPKITPKVVRSQ CCCCCCCCHHHCCCC | 24.15 | 23749301 | |
| 54 | Phosphorylation | NPAFLPGTNNNSNSN CCCCCCCCCCCCCCC | 32.60 | 21440633 | |
| 58 | Phosphorylation | LPGTNNNSNSNNNSS CCCCCCCCCCCCCCC | 43.70 | 21440633 | |
| 60 | Phosphorylation | GTNNNSNSNNNSSNE CCCCCCCCCCCCCCH | 40.53 | 20377248 | |
| 64 | Phosphorylation | NSNSNNNSSNEKEQL CCCCCCCCCCHHHHH | 36.34 | 21440633 | |
| 65 | Phosphorylation | SNSNNNSSNEKEQLS CCCCCCCCCHHHHHH | 51.65 | 21440633 | |
| 68 | Ubiquitination | NNNSSNEKEQLSFIN CCCCCCHHHHHHHCC | 55.82 | 23749301 | |
| 68 | Acetylation | NNNSSNEKEQLSFIN CCCCCCHHHHHHHCC | 55.82 | 24489116 | |
| 72 | Phosphorylation | SNEKEQLSFINPKTG CCHHHHHHHCCCCCC | 24.63 | 21440633 | |
| 120 | Acetylation | KEGRRVPKELAVENP CCCCCCCHHHHCCCH | 63.60 | 24489116 | |
| 177 | Acetylation | QLIGAATKFKGGKRQ EEEEEEEECCCHHHH | 40.11 | 24489116 | |
| 218 | Acetylation | DFDNIEFKKIPRVKG CCCCCCCCCCCCCCC | 36.68 | 24489116 | |
| 245 | Phosphorylation | FLMGHPMTKSVYETP CCCCCCCCCCHHCCC | 25.31 | 27017623 | |
| 246 | Acetylation | LMGHPMTKSVYETPK CCCCCCCCCHHCCCC | 31.50 | 24489116 | |
| 247 | Phosphorylation | MGHPMTKSVYETPKI CCCCCCCCHHCCCCC | 22.29 | 19823750 | |
| 249 | Phosphorylation | HPMTKSVYETPKITA CCCCCCHHCCCCCCH | 22.60 | 19823750 | |
| 251 | Phosphorylation | MTKSVYETPKITAAE CCCCHHCCCCCCHHH | 16.52 | 19823750 | |
| 253 | Acetylation | KSVYETPKITAAEKS CCHHCCCCCCHHHHH | 61.17 | 24489116 | |
| 255 | Phosphorylation | VYETPKITAAEKSFK HHCCCCCCHHHHHCC | 26.41 | 19823750 |
| 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 SEC65_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC65_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 SEC65_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND MASSSPECTROMETRY. | |
