| UniProt ID | SEH1_YEAST | |
|---|---|---|
| UniProt AC | P53011 | |
| Protein Name | Nucleoporin SEH1 | |
| Gene Name | SEH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 349 | |
| Subcellular Localization |
Nucleus, nuclear pore complex . Nucleus membrane Peripheral membrane protein Cytoplasmic side . Vacuole membrane Peripheral membrane protein . Nucleus membrane Peripheral membrane protein Nucleoplasmic side . Symmetric distribution. |
|
| Protein Description | Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.. | |
| Protein Sequence | MQPFDSGHDDLVHDVVYDFYGRHVATCSSDQHIKVFKLDKDTSNWELSDSWRAHDSSIVAIDWASPEYGRIIASASYDKTVKLWEEDPDQEECSGRRWNKLCTLNDSKGSLYSVKFAPAHLGLKLACLGNDGILRLYDALEPSDLRSWTLTSEMKVLSIPPANHLQSDFCLSWCPSRFSPEKLAVSALEQAIIYQRGKDGKLHVAAKLPGHKSLIRSISWAPSIGRWYQLIATGCKDGRIRIFKITEKLSPLASEESLTNSNMFDNSADVDMDAQGRSDSNTEEKAELQSNLQVELLSEHDDHNGEVWSVSWNLTGTILSSAGDDGKVRLWKATYSNEFKCMSVITAQQ | |
| 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 |
|---|---|---|---|---|---|
| 42 | Phosphorylation | VFKLDKDTSNWELSD EEEECCCCCCCEECC | 29.69 | 28889911 | |
| 43 | Phosphorylation | FKLDKDTSNWELSDS EEECCCCCCCEECCC | 50.51 | 19779198 | |
| 100 | Acetylation | CSGRRWNKLCTLNDS HCCCCCEEEEEEECC | 37.67 | 24489116 | |
| 100 | Ubiquitination | CSGRRWNKLCTLNDS HCCCCCEEEEEEECC | 37.67 | 23749301 | |
| 108 | Ubiquitination | LCTLNDSKGSLYSVK EEEEECCCCCEEEEE | 56.22 | 23749301 | |
| 110 | Phosphorylation | TLNDSKGSLYSVKFA EEECCCCCEEEEEEE | 28.06 | 19779198 | |
| 112 | Phosphorylation | NDSKGSLYSVKFAPA ECCCCCEEEEEEECC | 17.08 | 19779198 | |
| 115 | Acetylation | KGSLYSVKFAPAHLG CCCEEEEEEECCCCC | 29.84 | 24489116 | |
| 217 | Phosphorylation | GHKSLIRSISWAPSI CCHHHHHHHCCCCCC | 17.61 | 29688323 | |
| 219 | Phosphorylation | KSLIRSISWAPSIGR HHHHHHHCCCCCCCH | 20.59 | 29688323 | |
| 223 | Phosphorylation | RSISWAPSIGRWYQL HHHCCCCCCCHHHHH | 29.90 | 29688323 | |
| 250 | Phosphorylation | FKITEKLSPLASEES EEECCCCCCCCCCCC | 29.00 | 25752575 | |
| 254 | Phosphorylation | EKLSPLASEESLTNS CCCCCCCCCCCCCCC | 49.97 | 21551504 | |
| 257 | Phosphorylation | SPLASEESLTNSNMF CCCCCCCCCCCCCCC | 36.12 | 21440633 | |
| 259 | Phosphorylation | LASEESLTNSNMFDN CCCCCCCCCCCCCCC | 45.97 | 28889911 | |
| 261 | Phosphorylation | SEESLTNSNMFDNSA CCCCCCCCCCCCCCC | 25.16 | 25752575 | |
| 267 | Phosphorylation | NSNMFDNSADVDMDA CCCCCCCCCCCCCCC | 27.91 | 20377248 | |
| 278 | Phosphorylation | DMDAQGRSDSNTEEK CCCCCCCCCCCHHHH | 52.82 | 20377248 | |
| 280 | Phosphorylation | DAQGRSDSNTEEKAE CCCCCCCCCHHHHHH | 47.07 | 20377248 | |
| 282 | Phosphorylation | QGRSDSNTEEKAELQ CCCCCCCHHHHHHHH | 49.85 | 20377248 |
| 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 SEH1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEH1_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 SEH1_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 SER-250 AND SER-257, ANDMASS SPECTROMETRY. | |
