| UniProt ID | SEC63_YEAST | |
|---|---|---|
| UniProt AC | P14906 | |
| Protein Name | Protein translocation protein SEC63 | |
| Gene Name | SEC63 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 663 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein. Nucleus membrane Multi-pass membrane protein. Nucleus inner 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. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC63 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. May also be involved in SRP-dependent cotranslational translocation. Is essential for cell growth and for germination.. | |
| Protein Sequence | MPTNYEYDEASETWPSFILTGLLMVVGPMTLLQIYQIFFGANAEDGNSGKSKEFNEEVFKNLNEEYTSDEIKQFRRKFDKNSNKKSKIWSRRNIIIIVGWILVAILLQRINSNDAIKDAATKLFDPYEILGISTSASDRDIKSAYRKLSVKFHPDKLAKGLTPDEKSVMEETYVQITKAYESLTDELVRQNYLKYGHPDGPQSTSHGIALPRFLVDGSASPLLVVCYVALLGLILPYFVSRWWARTQSYTKKGIHNVTASNFVSNLVNYKPSEIVTTDLILHWLSFAHEFKQFFPDLQPTDFEKLLQDHINRRDSGKLNNAKFRIVAKCHSLLHGLLDIACGFRNLDIALGAINTFKCIVQAVPLTPNCQILQLPNVDKEHFITKTGDIHTLGKLFTLEDAKIGEVLGIKDQAKLNETLRVASHIPNLKIIKADFLVPGENQVTPSSTPYISLKVLVRSAKQPLIPTSLIPEENLTEPQDFESQRDPFAMMSKQPLVPYSFAPFFPTKRRGSWCCLVSSQKDGKILQTPIIIEKLSYKNLNDDKDFFDKRIKMDLTKHEKFDINDWEIGTIKIPLGQPAPETVGDFFFRVIVKSTDYFTTDLDITMNMKVRDSPAVEQVEVYSEEDDEYSTDDDETESDDESDASDYTDIDTDTEAEDDESPE | |
| 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 |
|---|---|---|---|---|---|
| 52 | Acetylation | DGNSGKSKEFNEEVF CCCCCCCHHHHHHHH | 70.57 | 24489116 | |
| 60 | Acetylation | EFNEEVFKNLNEEYT HHHHHHHHHHCCCCC | 66.74 | 24489116 | |
| 72 | Acetylation | EYTSDEIKQFRRKFD CCCHHHHHHHHHHHC | 41.14 | 24489116 | |
| 143 | Phosphorylation | ASDRDIKSAYRKLSV CCHHHHHHHHHHHHC | 30.76 | 27017623 | |
| 194 | Acetylation | LVRQNYLKYGHPDGP HHHHHCHHHCCCCCC | 38.53 | 24489116 | |
| 248 | Phosphorylation | RWWARTQSYTKKGIH HHHHHCCCCCCCCCC | 33.87 | 27017623 | |
| 249 | Phosphorylation | WWARTQSYTKKGIHN HHHHCCCCCCCCCCC | 16.86 | 27017623 | |
| 304 | Acetylation | LQPTDFEKLLQDHIN CCCCCHHHHHHHHHH | 55.26 | 24489116 | |
| 385 | Acetylation | DKEHFITKTGDIHTL CHHHEEECCCCCEEC | 45.77 | 22865919 | |
| 394 | Acetylation | GDIHTLGKLFTLEDA CCCEECCCEEECCCC | 43.47 | 24489116 | |
| 410 | Succinylation | IGEVLGIKDQAKLNE HHHHCCCCCHHHHHH | 41.82 | 23954790 | |
| 450 | Phosphorylation | VTPSSTPYISLKVLV CCCCCCCCEEHHHHH | 11.84 | 28889911 | |
| 467 | Phosphorylation | AKQPLIPTSLIPEEN CCCCCCCCCCCCCCC | 29.22 | 19779198 | |
| 468 | Phosphorylation | KQPLIPTSLIPEENL CCCCCCCCCCCCCCC | 20.96 | 19779198 | |
| 476 | Phosphorylation | LIPEENLTEPQDFES CCCCCCCCCCCCHHH | 58.14 | 19779198 | |
| 508 | Acetylation | FAPFFPTKRRGSWCC CCCCCCCCCCCCEEE | 40.09 | 24489116 | |
| 512 | Phosphorylation | FPTKRRGSWCCLVSS CCCCCCCCEEEEEEE | 18.35 | 17330950 | |
| 518 | Phosphorylation | GSWCCLVSSQKDGKI CCEEEEEEECCCCEE | 17.69 | 19823750 | |
| 519 | Phosphorylation | SWCCLVSSQKDGKIL CEEEEEEECCCCEEE | 33.50 | 19823750 | |
| 528 | Phosphorylation | KDGKILQTPIIIEKL CCCEEEECCEEEEEC | 17.01 | 27214570 | |
| 534 | Acetylation | QTPIIIEKLSYKNLN ECCEEEEECCCCCCC | 32.12 | 24489116 | |
| 544 | Acetylation | YKNLNDDKDFFDKRI CCCCCCCHHHHHHHH | 60.34 | 24489116 | |
| 549 | Acetylation | DDKDFFDKRIKMDLT CCHHHHHHHHCCCCC | 51.36 | 24489116 | |
| 560 | Acetylation | MDLTKHEKFDINDWE CCCCCCCCCCCCCCE | 48.32 | 24489116 | |
| 605 | Phosphorylation | FTTDLDITMNMKVRD EECCEEEEEECEECC | 11.36 | 28889911 | |
| 652 | Phosphorylation | SDYTDIDTDTEAEDD HHCCCCCCCCCCCCC | 45.19 | 28889911 | |
| 654 | Phosphorylation | YTDIDTDTEAEDDES CCCCCCCCCCCCCCC | 38.91 | 28889911 |
| 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 SEC63_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC63_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 SEC63_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 TYR-450; SER-512 ANDTHR-528, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASSSPECTROMETRY. | |
